ID TOLC_ECOLI Reviewed; 493 AA.
AC P02930; Q2M9G5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 3.
DT 10-MAY-2017, entry version 166.
DE RecName: Full=Outer membrane protein TolC;
DE AltName: Full=Multidrug efflux pump subunit TolC;
DE AltName: Full=Outer membrane factor TolC;
DE Flags: Precursor;
GN Name=tolC; Synonyms=colE1-i, mtcB, mukA, refI, toc, weeA;
GN OrderedLocusNames=b3035, JW5503;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6312426; DOI=10.1093/nar/11.18.6487;
RA Hackett J., Reeves P.;
RT "Primary structure of the tolC gene that codes for an outer membrane
RT protein of Escherichia coli K12.";
RL Nucleic Acids Res. 11:6487-6495(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2216730; DOI=10.1093/nar/18.18.5547;
RA Niki H., Imamura R., Ogura T., Hiraga S.;
RT "Nucleotide sequence of the tolC gene of Escherichia coli.";
RL Nucleic Acids Res. 18:5547-5547(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RC STRAIN=K12;
RX PubMed=6303857; DOI=10.1016/0014-5793(83)80518-3;
RA Hackett J., Misra R., Reeves P.;
RT "The TolC protein of Escherichia coli K12 is synthesised in a
RT precursor form.";
RL FEBS Lett. 156:307-310(1983).
RN [6]
RP PROTEIN SEQUENCE OF 23-34, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=6337123;
RA Morona R., Manning P.A., Reeves P.;
RT "Identification and characterization of the TolC protein, an outer
RT membrane protein from Escherichia coli.";
RL J. Bacteriol. 153:693-699(1983).
RN [7]
RP PROTEIN SEQUENCE OF 23-34.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded
RT in the genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [8]
RP PROTEIN SEQUENCE OF 23-27.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9629924; DOI=10.1002/elps.1150190539;
RA Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M.,
RA Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.;
RT "Extraction of membrane proteins by differential solubilization for
RT separation using two-dimensional gel electrophoresis.";
RL Electrophoresis 19:837-844(1998).
RN [9]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9044294; DOI=10.1046/j.1365-2958.1997.d01-1880.x;
RA Koronakis V., Li J., Koronakis E., Stauffer K.;
RT "Structure of TolC, the outer membrane component of the bacterial type
RT I efflux system, derived from two-dimensional crystals.";
RL Mol. Microbiol. 23:617-626(1997).
RN [10]
RP FUNCTION IN ACREF-TOLC EFFLUX SYSTEM.
RX PubMed=11274125; DOI=10.1128/JB.183.8.2646-2653.2001;
RA Kobayashi K., Tsukagoshi N., Aono R.;
RT "Suppression of hypersensitivity of Escherichia coli acrB mutant to
RT organic solvents by integrational activation of the acrEF operon with
RT the IS1 or IS2 element.";
RL J. Bacteriol. 183:2646-2653(2001).
RN [11]
RP FUNCTION IN ACRAB-TOLC EFFLUX SYSTEM, INTERACTION WITH ACRA, SUBUNIT,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=15228545; DOI=10.1111/j.1365-2958.2004.04158.x;
RA Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.;
RT "Interactions underlying assembly of the Escherichia coli AcrAB-TolC
RT multidrug efflux system.";
RL Mol. Microbiol. 53:697-706(2004).
RN [12]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.M506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [13]
RP FUNCTION IN MACAB-TOLC EFFLUX SYSTEM, SUBUNIT, AND INTERACTION WITH
RP MACA.
RX PubMed=18955484; DOI=10.1074/jbc.M806964200;
RA Lin H.T., Bavro V.N., Barrera N.P., Frankish H.M., Velamakanni S.,
RA van Veen H.W., Robinson C.V., Borges-Walmsley M.I., Walmsley A.R.;
RT "MacB ABC transporter is a dimer whose ATPase activity and macrolide-
RT binding capacity are regulated by the membrane fusion protein MacA.";
RL J. Biol. Chem. 284:1145-1154(2009).
RN [14]
RP SUBUNIT.
RX PubMed=19342493; DOI=10.1073/pnas.0900693106;
RA Symmons M.F., Bokma E., Koronakis E., Hughes C., Koronakis V.;
RT "The assembled structure of a complete tripartite bacterial multidrug
RT efflux pump.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7173-7178(2009).
RN [15]
RP INTERACTION WITH ACRA; EMRA AND MACA.
RX PubMed=19805313; DOI=10.1073/pnas.0906601106;
RA Tikhonova E.B., Dastidar V., Rybenkov V.V., Zgurskaya H.I.;
RT "Kinetic control of TolC recruitment by multidrug efflux complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16416-16421(2009).
RN [16]
RP INTERACTION WITH MACA.
RX PubMed=21325274; DOI=10.1074/jbc.M110.202598;
RA Xu Y., Song S., Moeller A., Kim N., Piao S., Sim S.H., Kang M., Yu W.,
RA Cho H.S., Chang I., Lee K., Ha N.C.;
RT "Functional implications of an intermeshing cogwheel-like interaction
RT between TolC and MacA in the action of macrolide-specific efflux pump
RT MacAB-TolC.";
RL J. Biol. Chem. 286:13541-13549(2011).
RN [17]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21778229; DOI=10.1074/jbc.M111.245696;
RA Fontaine F., Fuchs R.T., Storz G.;
RT "Membrane localization of small proteins in Escherichia coli.";
RL J. Biol. Chem. 286:32464-32474(2011).
RN [18]
RP FUNCTION IN COLICIN E1 IMPORT.
RX PubMed=23176499; DOI=10.1042/BST20120211;
RA Zakharov S.D., Sharma O., Zhalnina M., Yamashita E., Cramer W.A.;
RT "Pathways of colicin import: utilization of BtuB, OmpF porin and the
RT TolC drug-export protein.";
RL Biochem. Soc. Trans. 40:1463-1468(2012).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-450, AND DOMAIN.
RX PubMed=10879525; DOI=10.1038/35016007;
RA Koronakis V., Sharff A., Koronakis E., Luisi B., Hughes C.;
RT "Crystal structure of the bacterial membrane protein TolC central to
RT multidrug efflux and protein export.";
RL Nature 405:914-919(2000).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 23-493 IN COMPLEX WITH
RP HEXAAMMINECOBALT(3+), ENZYME REGULATION, AND MUTAGENESIS OF ASP-393
RP AND ASP-396.
RX PubMed=15342230; DOI=10.1016/j.jmb.2004.07.088;
RA Higgins M.K., Eswaran J., Edwards P., Schertler G.F., Hughes C.,
RA Koronakis V.;
RT "Structure of the ligand-blocked periplasmic entrance of the bacterial
RT multidrug efflux protein TolC.";
RL J. Mol. Biol. 342:697-702(2004).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 3-450 OF MUTANT
RP PHE-384/GLU-389, AND MUTAGENESIS OF TYR-384 AND ARG-389.
RX PubMed=18406332; DOI=10.1016/j.molcel.2008.02.015;
RA Bavro V.N., Pietras Z., Furnham N., Perez-Cano L., Fernandez-Recio J.,
RA Pei X.Y., Misra R., Luisi B.;
RT "Assembly and channel opening in a bacterial drug efflux machine.";
RL Mol. Cell 30:114-121(2008).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 23-450 OF MUTANTS.
RX PubMed=21245342; DOI=10.1073/pnas.1012588108;
RA Pei X.Y., Hinchliffe P., Symmons M.F., Koronakis E., Benz R.,
RA Hughes C., Koronakis V.;
RT "Structures of sequential open states in a symmetrical opening
RT transition of the TolC exit duct.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2112-2117(2011).
CC -!- FUNCTION: Outer membrane channel, which is required for the
CC function of several efflux systems such as AcrAB-TolC, AcrEF-TolC,
CC EmrAB-TolC and MacAB-TolC. These systems are involved in export of
CC antibiotics and other toxic compounds from the cell. TolC is also
CC involved in import of colicin E1 into the cells.
CC {ECO:0000269|PubMed:11274125, ECO:0000269|PubMed:15228545,
CC ECO:0000269|PubMed:18955484, ECO:0000269|PubMed:23176499,
CC ECO:0000269|PubMed:6337123}.
CC -!- ENZYME REGULATION: In vitro, inhibited by hexaamminecobalt(3+).
CC {ECO:0000269|PubMed:15342230}.
CC -!- SUBUNIT: Homotrimer. Part of tripartite efflux systems, which are
CC composed of an inner membrane transporter, a periplasmic membrane
CC fusion protein, and an outer membrane component, TolC. The
CC complexes form a large protein conduit and can translocate
CC molecules across both the inner and outer membranes. TolC
CC interacts with the membrane fusion proteins AcrA, EmrA and MacA.
CC {ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:15342230,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:18955484,
CC ECO:0000269|PubMed:19342493, ECO:0000269|PubMed:19805313,
CC ECO:0000269|PubMed:21325274, ECO:0000269|PubMed:9044294}.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-875614, EBI-875614;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:21778229, ECO:0000269|PubMed:6337123,
CC ECO:0000269|PubMed:9044294}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:16079137,
CC ECO:0000269|PubMed:21778229, ECO:0000269|PubMed:6337123,
CC ECO:0000269|PubMed:9044294}.
CC -!- DOMAIN: Forms a continuous, solvent-accessible conduit: a
CC 'channel-tunnel' over 140 Angstroms long that spans both the outer
CC membrane and periplasmic space. The periplasmic or proximal end of
CC the tunnel is sealed by sets of coiled helices.
CC {ECO:0000269|PubMed:10879525}.
CC -!- DISRUPTION PHENOTYPE: Cannot grow on efflux substrates novobiocin
CC or fusidic acid. {ECO:0000269|PubMed:15228545}.
CC -!- SIMILARITY: Belongs to the outer membrane factor (OMF) (TC 1.B.17)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69203.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC Sequence=CAA24751.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC Sequence=CAA37982.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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DR EMBL; X00016; CAA24914.1; -; Genomic_DNA.
DR EMBL; X54049; CAA37982.1; ALT_INIT; Genomic_DNA.
DR EMBL; U28377; AAA69203.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76071.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77091.1; -; Genomic_DNA.
DR EMBL; V01505; CAA24751.1; ALT_INIT; Genomic_DNA.
DR PIR; A65091; MMECTC.
DR RefSeq; NP_417507.2; NC_000913.3.
DR RefSeq; WP_000735278.1; NZ_LN832404.1.
DR PDB; 1EK9; X-ray; 2.10 A; A/B/C=23-450.
DR PDB; 1TQQ; X-ray; 2.75 A; A/B/C=23-493.
DR PDB; 2VDD; X-ray; 3.30 A; A/B/C=1-450.
DR PDB; 2VDE; X-ray; 3.20 A; A/B/C=1-450.
DR PDB; 2WMZ; X-ray; 2.90 A; A/B/C=23-450.
DR PDB; 2XMN; X-ray; 2.85 A; A/B/C=23-450.
DR PDBsum; 1EK9; -.
DR PDBsum; 1TQQ; -.
DR PDBsum; 2VDD; -.
DR PDBsum; 2VDE; -.
DR PDBsum; 2WMZ; -.
DR PDBsum; 2XMN; -.
DR ProteinModelPortal; P02930; -.
DR SMR; P02930; -.
DR BioGrid; 4263248; 380.
DR DIP; DIP-11007N; -.
DR IntAct; P02930; 5.
DR STRING; 511145.b3035; -.
DR DrugBank; DB03350; Cobalt Hexammine Ion.
DR TCDB; 1.B.17.1.1; the outer membrane factor (omf) family.
DR SWISS-2DPAGE; P02930; -.
DR EPD; P02930; -.
DR PaxDb; P02930; -.
DR PRIDE; P02930; -.
DR EnsemblBacteria; AAC76071; AAC76071; b3035.
DR EnsemblBacteria; BAE77091; BAE77091; BAE77091.
DR GeneID; 947521; -.
DR KEGG; ecj:JW5503; -.
DR KEGG; eco:b3035; -.
DR PATRIC; 32121480; VBIEscCol129921_3127.
DR EchoBASE; EB1002; -.
DR EcoGene; EG11009; tolC.
DR eggNOG; ENOG4105DFG; Bacteria.
DR eggNOG; COG1538; LUCA.
DR HOGENOM; HOG000283506; -.
DR InParanoid; P02930; -.
DR KO; K12340; -.
DR OMA; AMSQAEN; -.
DR PhylomeDB; P02930; -.
DR BioCyc; EcoCyc:EG11009-MONOMER; -.
DR BioCyc; MetaCyc:EG11009-MONOMER; -.
DR EvolutionaryTrace; P02930; -.
DR PRO; PR:P02930; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IDA:CAFA.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005216; F:ion channel activity; IDA:CAFA.
DR GO; GO:0015288; F:porin activity; IDA:EcoCyc.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:CAFA.
DR GO; GO:0042930; P:enterobactin transport; IGI:EcoliWiki.
DR GO; GO:0034220; P:ion transmembrane transport; IDA:CAFA.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR GO; GO:0014070; P:response to organic cyclic compound; IMP:EcoliWiki.
DR InterPro; IPR003423; OMP_efflux.
DR InterPro; IPR010130; T1SS_OMP_TolC.
DR PANTHER; PTHR30026:SF10; PTHR30026:SF10; 1.
DR Pfam; PF02321; OEP; 2.
DR TIGRFAMs; TIGR01844; type_I_sec_TolC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell outer membrane;
KW Complete proteome; Direct protein sequencing; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1 22 {ECO:0000269|PubMed:6337123,
FT ECO:0000269|PubMed:9298646,
FT ECO:0000269|PubMed:9629924}.
FT CHAIN 23 493 Outer membrane protein TolC.
FT /FTId=PRO_0000013352.
FT TOPO_DOM 23 62 Periplasmic.
FT TRANSMEM 63 74 Beta stranded; Name=S1.
FT TOPO_DOM 75 82 Extracellular.
FT TRANSMEM 83 96 Beta stranded; Name=S2.
FT TOPO_DOM 97 268 Periplasmic.
FT TRANSMEM 269 279 Beta stranded; Name=S4.
FT TOPO_DOM 280 300 Extracellular.
FT TRANSMEM 301 311 Beta stranded; Name=S5.
FT TOPO_DOM 312 493 Periplasmic.
FT REPEAT 23 230 1.
FT REPEAT 231 446 2.
FT MUTAGEN 384 384 Y->F: Partial channel opening. Increases
FT sensitivity to vancomycin, by allowing
FT its passive diffusion across the outer
FT membrane; when associated with E-389.
FT {ECO:0000269|PubMed:18406332}.
FT MUTAGEN 389 389 R->E: Partial channel opening. Increases
FT sensitivity to vancomycin, by allowing
FT its passive diffusion across the outer
FT membrane; when associated with F-382.
FT {ECO:0000269|PubMed:18406332}.
FT MUTAGEN 393 393 D->A: Decreases inhibition by
FT hexaamminecobalt(3+).
FT {ECO:0000269|PubMed:15342230}.
FT MUTAGEN 396 396 D->A: Decreases inhibition by
FT hexaamminecobalt(3+).
FT {ECO:0000269|PubMed:15342230}.
FT CONFLICT 178 178 N -> K (in Ref. 1; CAA24914).
FT {ECO:0000305}.
FT CONFLICT 191 191 V -> L (in Ref. 2; CAA37982).
FT {ECO:0000305}.
FT CONFLICT 203 204 QL -> HV (in Ref. 1; CAA24914).
FT {ECO:0000305}.
FT CONFLICT 214 215 EL -> GT (in Ref. 1; CAA24914).
FT {ECO:0000305}.
FT CONFLICT 258 270 QIRQAQDGHLPTL -> KFARRRMVTYRLW (in Ref.
FT 1; CAA24914). {ECO:0000305}.
FT CONFLICT 278 295 ISDTSYSGSKTRGAAGTQ -> FLTPLIAVRKPCAAVP
FT (in Ref. 1; CAA24914). {ECO:0000305}.
FT CONFLICT 325 325 K -> T (in Ref. 1; CAA24914).
FT {ECO:0000305}.
FT CONFLICT 335 354 SEQLESAHRSVVQTVRSSFN -> ASTWKVPIVASCQRAFC
FT FS (in Ref. 1; CAA24914). {ECO:0000305}.
FT CONFLICT 365 370 AYKQAV -> RYTQAA (in Ref. 1; CAA24914).
FT {ECO:0000305}.
FT CONFLICT 400 411 TLYNAKQELANA -> SCTAQARAGNP (in Ref. 1;
FT CAA24914). {ECO:0000305}.
FT CONFLICT 445 445 V -> I (in Ref. 1; CAA24914).
FT {ECO:0000305}.
FT HELIX 25 35 {ECO:0000244|PDB:1EK9}.
FT HELIX 37 57 {ECO:0000244|PDB:1EK9}.
FT HELIX 58 60 {ECO:0000244|PDB:1EK9}.
FT STRAND 63 75 {ECO:0000244|PDB:1EK9}.
FT STRAND 77 79 {ECO:0000244|PDB:1EK9}.
FT STRAND 83 98 {ECO:0000244|PDB:1EK9}.
FT HELIX 100 167 {ECO:0000244|PDB:1EK9}.
FT STRAND 168 170 {ECO:0000244|PDB:2VDE}.
FT HELIX 173 208 {ECO:0000244|PDB:1EK9}.
FT STRAND 213 218 {ECO:0000244|PDB:1EK9}.
FT TURN 220 222 {ECO:0000244|PDB:1EK9}.
FT HELIX 231 241 {ECO:0000244|PDB:1EK9}.
FT HELIX 243 263 {ECO:0000244|PDB:1EK9}.
FT HELIX 264 266 {ECO:0000244|PDB:1EK9}.
FT STRAND 269 279 {ECO:0000244|PDB:1EK9}.
FT STRAND 282 285 {ECO:0000244|PDB:1EK9}.
FT STRAND 288 291 {ECO:0000244|PDB:1EK9}.
FT STRAND 293 297 {ECO:0000244|PDB:2XMN}.
FT STRAND 302 316 {ECO:0000244|PDB:1EK9}.
FT HELIX 319 385 {ECO:0000244|PDB:1EK9}.
FT STRAND 386 388 {ECO:0000244|PDB:2VDD}.
FT HELIX 391 426 {ECO:0000244|PDB:1EK9}.
FT HELIX 431 439 {ECO:0000244|PDB:1EK9}.
FT STRAND 441 448 {ECO:0000244|PDB:1EK9}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 27 209 ipfam:OEP [T]
FT MYHIT 232 427 ipfam:OEP [T]
SQ SEQUENCE 493 AA; 53741 MW; 6F97B4C62A848FE1 CRC64;
MKKLLPILIG LSLSGFSSLS QAENLMQVYQ QARLSNPELR KSAADRDAAF EKINEARSPL
LPQLGLGADY TYSNGYRDAN GINSNATSAS LQLTQSIFDM SKWRALTLQE KAAGIQDVTY
QTDQQTLILN TATAYFNVLN AIDVLSYTQA QKEAIYRQLD QTTQRFNVGL VAITDVQNAR
AQYDTVLANE VTARNNLDNA VEQLRQITGN YYPELAALNV ENFKTDKPQP VNALLKEAEK
RNLSLLQARL SQDLAREQIR QAQDGHLPTL DLTASTGISD TSYSGSKTRG AAGTQYDDSN
MGQNKVGLSF SLPIYQGGMV NSQVKQAQYN FVGASEQLES AHRSVVQTVR SSFNNINASI
SSINAYKQAV VSAQSSLDAM EAGYSVGTRT IVDVLDATTT LYNAKQELAN ARYNYLINQL
NIKSALGTLN EQDLLALNNA LSKPVSTNPE NVAPQTPEQN AIADGYAPDS PAPVVQQTSA
RTTTSNGHNP FRN
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