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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Cytosol aminopeptidase; EC=3.4.11.1; AltName: Full=Aminopeptidase A/I; AltName: Full=Leucine aminopeptidase; Short=LAP; EC=3.4.11.10; AltName: Full=Leucyl aminopeptidase; |
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| MyHits synonyms | AMPA_ECOLI , P68767 , P11648 , Q2M649 , 643DED17EAC44DCD |
 Legends: 1, ACT_SITE {ECO:0000255}; 2, Manganese 2. {ECO:0000305}; 3, Manganese 1. {ECO:0000305}; 4, MUTAGEN E->A: Loss of activity. {ECO:0000269|PubMed:8057849}; 5, ipat:CYTOSOL_AP [T]; 6, STRAND {ECO:0000244|PDB:1GYT}; 7, HELIX {ECO:0000244|PDB:1GYT}; 8, TURN {ECO:0000244|PDB:1GYT}.
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ID AMPA_ECOLI Reviewed; 503 AA.
AC P68767; P11648; Q2M649;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 18-JAN-2017, entry version 108.
DE RecName: Full=Cytosol aminopeptidase;
DE EC=3.4.11.1;
DE AltName: Full=Aminopeptidase A/I;
DE AltName: Full=Leucine aminopeptidase;
DE Short=LAP;
DE EC=3.4.11.10;
DE AltName: Full=Leucyl aminopeptidase;
GN Name=pepA; Synonyms=carP, xerB; OrderedLocusNames=b4260, JW4217;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX PubMed=2670557;
RA Stirling C.J., Colloms S., Collins J.F., Szatmari G., Sherratt D.J.;
RT "xerB, an Escherichia coli gene required for plasmid ColE1 site-
RT specific recombination, is identical to pepA, encoding aminopeptidase
RT A, a protein with substantial similarity to bovine lens leucine
RT aminopeptidase.";
RL EMBO J. 8:1623-1627(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7616564; DOI=10.1006/jmbi.1995.0385;
RA Charlier D., Hassanzadeh G., Kholti A., Gigot D., Pierard A.,
RA Glansdorff N.;
RT "carP, involved in pyrimidine regulation of the Escherichia coli
RT carbamoylphosphate synthetase operon encodes a sequence-specific DNA-
RT binding protein identical to XerB and PepA, also required for
RT resolution of ColEI multimers.";
RL J. Mol. Biol. 250:392-406(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT region from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [4]
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 [5]
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 [6]
RP MUTAGENESIS OF GLU-354.
RX PubMed=8057849; DOI=10.1111/j.1365-2958.1994.tb01013.x;
RA McCulloch R., Burke M.E., Sherratt D.J.;
RT "Peptidase activity of Escherichia coli aminopeptidase A is not
RT required for its role in Xer site-specific recombination.";
RL Mol. Microbiol. 12:241-251(1994).
RN [7]
RP FUNCTION IN PEPTIDE DEGRADATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926;
RX PubMed=20067529; DOI=10.1111/j.1574-6968.2009.01879.x;
RA Hayashi M., Tabata K., Yagasaki M., Yonetani Y.;
RT "Effect of multidrug-efflux transporter genes on dipeptide resistance
RT and overproduction in Escherichia coli.";
RL FEMS Microbiol. Lett. 304:12-19(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=10449417; DOI=10.1093/emboj/18.16.4513;
RA Strater N., Sherratt D.J., Colloms S.D.;
RT "X-ray structure of aminopeptidase A from Escherichia coli and a model
RT for the nucleoprotein complex in Xer site-specific recombination.";
RL EMBO J. 18:4513-4522(1999).
CC -!- FUNCTION: Probably involved in the processing and regular turnover
CC of intracellular proteins (PubMed:20067529). Catalyzes the removal
CC of unsubstituted N-terminal amino acids from various peptides.
CC Required for plasmid ColE1 site-specific recombination but not in
CC its aminopeptidase activity. Could act as a structural component
CC of the putative nucleoprotein complex in which the Xer
CC recombination reaction takes place (PubMed:8057849).
CC {ECO:0000269|PubMed:8057849, ECO:0000305|PubMed:20067529}.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-
CC Yaa-, in which Xaa is preferably Leu, but may be other amino acids
CC including Pro although not Arg or Lys, and Yaa may be Pro. Amino
CC acid amides and methyl esters are also readily hydrolyzed, but
CC rates on arylamides are exceedingly low.
CC -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
CC preferentially leucine, but not glutamic or aspartic acids.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- ENZYME REGULATION: Inhibited by zinc and EDTA.
CC -!- SUBUNIT: Homohexamer.
CC -!- DISRUPTION PHENOTYPE: A quadruple peptidase disruption (pepA,
CC pepB, pepD and pepN) does not grow in M9 minimal medium, grows
CC better when supplemented with casamino acids (PubMed:20067529).
CC {ECO:0000269|PubMed:20067529}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family. {ECO:0000305}.
CC -!- CAUTION: The ligation for manganese is based on the ligation for
CC zinc, an inhibitor, in the crystallographic structure reported in
CC PubMed:10449417. The ligation for manganese in the active form of
CC the enzyme may differ. {ECO:0000305}.
DR EMBL; X15130; CAA33225.1; -; Genomic_DNA.
DR EMBL; X86443; CAA60164.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97157.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77217.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78257.1; -; Genomic_DNA.
DR PIR; S04462; APECA.
DR RefSeq; NP_418681.1; NC_000913.3.
DR RefSeq; WP_000397144.1; NZ_LN832404.1.
DR PDB; 1GYT; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-503.
DR PDBsum; 1GYT; -.
DR ProteinModelPortal; P68767; -.
DR SMR; P68767; -.
DR BioGrid; 4262726; 40.
DR DIP; DIP-47860N; -.
DR IntAct; P68767; 5.
DR STRING; 511145.b4260; -.
DR MEROPS; M17.003; -.
DR MoonProt; P68767; -.
DR EPD; P68767; -.
DR PaxDb; P68767; -.
DR PRIDE; P68767; -.
DR EnsemblBacteria; AAC77217; AAC77217; b4260.
DR EnsemblBacteria; BAE78257; BAE78257; BAE78257.
DR GeneID; 948791; -.
DR KEGG; ecj:JW4217; -.
DR KEGG; eco:b4260; -.
DR PATRIC; 32124091; VBIEscCol129921_4390.
DR EchoBASE; EB0688; -.
DR EcoGene; EG10694; pepA.
DR eggNOG; ENOG4105BZ6; Bacteria.
DR eggNOG; COG0260; LUCA.
DR HOGENOM; HOG000243132; -.
DR InParanoid; P68767; -.
DR KO; K01255; -.
DR OMA; AICEMKL; -.
DR PhylomeDB; P68767; -.
DR BioCyc; EcoCyc:EG10694-MONOMER; -.
DR BioCyc; ECOL316407:JW4217-MONOMER; -.
DR BioCyc; MetaCyc:EG10694-MONOMER; -.
DR EvolutionaryTrace; P68767; -.
DR PRO; PR:P68767; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:EcoliWiki.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0001073; F:transcription antitermination factor activity, DNA binding; IMP:EcoliWiki.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0043171; P:peptide catabolic process; IMP:EcoliWiki.
DR GO; GO:0006276; P:plasmid maintenance; IMP:EcoliWiki.
DR GO; GO:0042150; P:plasmid recombination; IMP:EcoliWiki.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:EcoCyc.
DR CDD; cd00433; Peptidase_M17; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963; PTHR11963; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Complete proteome;
KW Direct protein sequencing; Hydrolase; Manganese; Metal-binding;
KW Protease; Reference proteome.
FT CHAIN 1 503 Cytosol aminopeptidase.
FT /FTId=PRO_0000165750.
FT ACT_SITE 282 282 {ECO:0000255}.
FT ACT_SITE 356 356 {ECO:0000255}.
FT METAL 270 270 Manganese 2. {ECO:0000305}.
FT METAL 275 275 Manganese 1. {ECO:0000305}.
FT METAL 275 275 Manganese 2. {ECO:0000305}.
FT METAL 293 293 Manganese 2. {ECO:0000305}.
FT METAL 352 352 Manganese 1. {ECO:0000305}.
FT METAL 354 354 Manganese 1. {ECO:0000305}.
FT METAL 354 354 Manganese 2. {ECO:0000305}.
FT MUTAGEN 354 354 E->A: Loss of activity.
FT {ECO:0000269|PubMed:8057849}.
FT STRAND 2 6 {ECO:0000244|PDB:1GYT}.
FT HELIX 10 12 {ECO:0000244|PDB:1GYT}.
FT STRAND 18 23 {ECO:0000244|PDB:1GYT}.
FT TURN 24 26 {ECO:0000244|PDB:1GYT}.
FT HELIX 30 36 {ECO:0000244|PDB:1GYT}.
FT STRAND 39 41 {ECO:0000244|PDB:1GYT}.
FT HELIX 42 49 {ECO:0000244|PDB:1GYT}.
FT STRAND 59 64 {ECO:0000244|PDB:1GYT}.
FT STRAND 69 77 {ECO:0000244|PDB:1GYT}.
FT HELIX 86 102 {ECO:0000244|PDB:1GYT}.
FT STRAND 106 110 {ECO:0000244|PDB:1GYT}.
FT HELIX 112 114 {ECO:0000244|PDB:1GYT}.
FT HELIX 122 137 {ECO:0000244|PDB:1GYT}.
FT STRAND 156 160 {ECO:0000244|PDB:1GYT}.
FT HELIX 164 166 {ECO:0000244|PDB:1GYT}.
FT HELIX 167 192 {ECO:0000244|PDB:1GYT}.
FT TURN 195 197 {ECO:0000244|PDB:1GYT}.
FT HELIX 200 213 {ECO:0000244|PDB:1GYT}.
FT TURN 214 217 {ECO:0000244|PDB:1GYT}.
FT STRAND 218 223 {ECO:0000244|PDB:1GYT}.
FT HELIX 225 230 {ECO:0000244|PDB:1GYT}.
FT HELIX 234 241 {ECO:0000244|PDB:1GYT}.
FT STRAND 243 245 {ECO:0000244|PDB:1GYT}.
FT STRAND 248 255 {ECO:0000244|PDB:1GYT}.
FT STRAND 265 275 {ECO:0000244|PDB:1GYT}.
FT HELIX 287 294 {ECO:0000244|PDB:1GYT}.
FT HELIX 295 310 {ECO:0000244|PDB:1GYT}.
FT STRAND 313 325 {ECO:0000244|PDB:1GYT}.
FT STRAND 337 339 {ECO:0000244|PDB:1GYT}.
FT STRAND 345 347 {ECO:0000244|PDB:1GYT}.
FT HELIX 355 365 {ECO:0000244|PDB:1GYT}.
FT HELIX 366 369 {ECO:0000244|PDB:1GYT}.
FT STRAND 372 378 {ECO:0000244|PDB:1GYT}.
FT HELIX 382 388 {ECO:0000244|PDB:1GYT}.
FT TURN 389 391 {ECO:0000244|PDB:1GYT}.
FT STRAND 392 398 {ECO:0000244|PDB:1GYT}.
FT HELIX 400 413 {ECO:0000244|PDB:1GYT}.
FT STRAND 417 419 {ECO:0000244|PDB:1GYT}.
FT HELIX 424 427 {ECO:0000244|PDB:1GYT}.
FT HELIX 428 430 {ECO:0000244|PDB:1GYT}.
FT STRAND 433 439 {ECO:0000244|PDB:1GYT}.
FT HELIX 446 455 {ECO:0000244|PDB:1GYT}.
FT STRAND 463 467 {ECO:0000244|PDB:1GYT}.
FT TURN 469 471 {ECO:0000244|PDB:1GYT}.
FT STRAND 472 474 {ECO:0000244|PDB:1GYT}.
FT HELIX 476 478 {ECO:0000244|PDB:1GYT}.
FT HELIX 486 496 {ECO:0000244|PDB:1GYT}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 350 357 ipat:CYTOSOL_AP [T]
FT MYHIT 3 498 ihamap:Cytosol_peptidase_M17 [T]
FT MYHIT 186 489 ipfam:Peptidase_M17 [T]
FT MYHIT 19 147 ipfam:Peptidase_M17_N [T]
SQ SEQUENCE 503 AA; 54880 MW; 643DED17EAC44DCD CRC64;
MEFSVKSGSP EKQRSACIVV GVFEPRRLSP IAEQLDKISD GYISALLRRG ELEGKPGQTL
LLHHVPNVLS ERILLIGCGK ERELDERQYK QVIQKTINTL NDTGSMEAVC FLTELHVKGR
NNYWKVRQAV ETAKETLYSF DQLKTNKSEP RRPLRKMVFN VPTRRELTSG ERAIQHGLAI
AAGIKAAKDL GNMPPNICNA AYLASQARQL ADSYSKNVIT RVIGEQQMKE LGMHSYLAVG
QGSQNESLMS VIEYKGNASE DARPIVLVGK GLTFDSGGIS IKPSEGMDEM KYDMCGAAAV
YGVMRMVAEL QLPINVIGVL AGCENMPGGR AYRPGDVLTT MSGQTVEVLN TDAEGRLVLC
DVLTYVERFE PEAVIDVATL TGACVIALGH HITGLMANHN PLAHELIAAS EQSGDRAWRL
PLGDEYQEQL ESNFADMANI GGRPGGAITA GCFLSRFTRK YNWAHLDIAG TAWRSGKAKG
ATGRPVALLA QFLLNRAGFN GEE
//
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