MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
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
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=Cell division protein FtsP {ECO:0000255|HAMAP-Rule:MF_00915}; Flags: Precursor; |
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| MyHits synonyms | FTSP_ECOLI , P26648 , Q2M9I3 , C843A5A4CB146688 |
 Legends: 1, SIGNAL Tat-type signal. {ECO:0000255|HAMAP- Rule:MF_00915, ECO:0000269|PubMed:9298646}; 2, Plastocyanin-like. {ECO:0000255|HAMAP- Rule:MF_00915}; 3, iprf:TAT [T]; 4, ipfam:Cu-oxidase [T]; 5, STRAND {ECO:0000244|PDB:2UXV}; 6, STRAND {ECO:0000244|PDB:2UXT}; 7, HELIX {ECO:0000244|PDB:2UXT}; 8, TURN {ECO:0000244|PDB:2UXT}.
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ID FTSP_ECOLI Reviewed; 470 AA.
AC P26648; Q2M9I3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 15-MAR-2017, entry version 134.
DE RecName: Full=Cell division protein FtsP {ECO:0000255|HAMAP-Rule:MF_00915};
DE Flags: Precursor;
GN Name=ftsP {ECO:0000255|HAMAP-Rule:MF_00915}; Synonyms=sufI;
GN OrderedLocusNames=b3017, JW2985;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
RX PubMed=1557036;
RA Coleman J.;
RT "Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-
RT 3-phosphate acyltransferase (plsC).";
RL Mol. Gen. Genet. 232:295-303(1992).
RN [4]
RP PROTEIN SEQUENCE OF 28-39.
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 [5]
RP SUBCELLULAR LOCATION, AND EXPORT VIA THE TAT-SYSTEM.
RC STRAIN=K12;
RX PubMed=10593889; DOI=10.1074/jbc.274.51.36073;
RA Sargent F., Stanley N.R., Berks B.C., Palmer T.;
RT "Sec-independent protein translocation in Escherichia coli. A distinct
RT and pivotal role for the TatB protein.";
RL J. Biol. Chem. 274:36073-36082(1999).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=K12;
RX PubMed=17766410; DOI=10.1128/JB.00773-07;
RA Samaluru H., Saisree L., Reddy M.;
RT "Role of SufI (FtsP) in cell division of Escherichia coli: evidence
RT for its involvement in stabilizing the assembly of the divisome.";
RL J. Bacteriol. 189:8044-8052(2007).
RN [7]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.M610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P.,
RA Ribnicky B., Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine
RT translocation signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 28-470, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=K12;
RX PubMed=19135451; DOI=10.1016/j.jmb.2008.12.043;
RA Tarry M., Arends S.J., Roversi P., Piette E., Sargent F., Berks B.C.,
RA Weiss D.S., Lea S.M.;
RT "The Escherichia coli cell division protein and model Tat substrate
RT SufI (FtsP) localizes to the septal ring and has a multicopper
RT oxidase-like structure.";
RL J. Mol. Biol. 386:504-519(2009).
CC -!- FUNCTION: Cell division protein that is required for growth during
CC stress conditions. May be involved in protecting or stabilizing
CC the divisomal assembly under conditions of stress.
CC {ECO:0000255|HAMAP-Rule:MF_00915, ECO:0000269|PubMed:17766410}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00915,
CC ECO:0000269|PubMed:10593889, ECO:0000269|PubMed:19135451}.
CC Note=Localizes to the division septum. Localization requires FtsZ,
CC FtsQ, FtsL and FtsN.
CC -!- PTM: Exported by the Tat system. The position of the signal
CC peptide cleavage has been experimentally proven. Can also be
CC exported by the Sec system.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are sensitive to
CC oxidative stress and DNA damage at high temperature. They also
CC exhibit filamentation. {ECO:0000269|PubMed:17766410}.
CC -!- MISCELLANEOUS: Is used as a model substrate in studies of the
CC twin-arginine translocation (Tat) protein transport system.
CC -!- SIMILARITY: Belongs to the FtsP family. {ECO:0000255|HAMAP-
CC Rule:MF_00915}.
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DR EMBL; U28377; AAA69185.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76053.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77073.1; -; Genomic_DNA.
DR EMBL; M63491; AAA24398.1; -; Genomic_DNA.
DR PIR; G65088; G65088.
DR RefSeq; NP_417489.1; NC_000913.3.
DR RefSeq; WP_000059388.1; NZ_LN832404.1.
DR PDB; 2UXT; X-ray; 1.90 A; A/B=28-470.
DR PDB; 2UXV; X-ray; 2.61 A; A/B=28-470.
DR PDBsum; 2UXT; -.
DR PDBsum; 2UXV; -.
DR ProteinModelPortal; P26648; -.
DR SMR; P26648; -.
DR BioGrid; 4260932; 56.
DR DIP; DIP-10942N; -.
DR IntAct; P26648; 7.
DR STRING; 511145.b3017; -.
DR PaxDb; P26648; -.
DR PRIDE; P26648; -.
DR EnsemblBacteria; AAC76053; AAC76053; b3017.
DR EnsemblBacteria; BAE77073; BAE77073; BAE77073.
DR GeneID; 944982; -.
DR KEGG; ecj:JW2985; -.
DR KEGG; eco:b3017; -.
DR PATRIC; 32121448; VBIEscCol129921_3111.
DR EchoBASE; EB1350; -.
DR EcoGene; EG11376; ftsP.
DR eggNOG; ENOG4107TZ2; Bacteria.
DR eggNOG; COG2132; LUCA.
DR HOGENOM; HOG000096435; -.
DR InParanoid; P26648; -.
DR KO; K04753; -.
DR OMA; PSYEHFP; -.
DR PhylomeDB; P26648; -.
DR BioCyc; EcoCyc:EG11376-MONOMER; -.
DR EvolutionaryTrace; P26648; -.
DR PRO; PR:P26648; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IMP:CACAO.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:InterPro.
DR Gene3D; 2.60.40.420; -; 3.
DR HAMAP; MF_00915; FtsP; 1.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_2.
DR InterPro; IPR011707; Cu-oxidase_3.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR026589; FtsP.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; SSF49503; 3.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Complete proteome;
KW Direct protein sequencing; Periplasm; Reference proteome; Signal.
FT SIGNAL 1 27 Tat-type signal. {ECO:0000255|HAMAP-
FT Rule:MF_00915,
FT ECO:0000269|PubMed:9298646}.
FT CHAIN 28 470 Cell division protein FtsP.
FT /FTId=PRO_0000002993.
FT DOMAIN 68 164 Plastocyanin-like. {ECO:0000255|HAMAP-
FT Rule:MF_00915}.
FT STRAND 39 42 {ECO:0000244|PDB:2UXV}.
FT STRAND 43 45 {ECO:0000244|PDB:2UXT}.
FT STRAND 48 54 {ECO:0000244|PDB:2UXT}.
FT HELIX 57 59 {ECO:0000244|PDB:2UXT}.
FT STRAND 61 65 {ECO:0000244|PDB:2UXT}.
FT STRAND 68 70 {ECO:0000244|PDB:2UXT}.
FT STRAND 73 75 {ECO:0000244|PDB:2UXT}.
FT STRAND 78 82 {ECO:0000244|PDB:2UXT}.
FT STRAND 86 93 {ECO:0000244|PDB:2UXT}.
FT STRAND 95 97 {ECO:0000244|PDB:2UXT}.
FT STRAND 101 104 {ECO:0000244|PDB:2UXT}.
FT HELIX 110 112 {ECO:0000244|PDB:2UXT}.
FT HELIX 116 118 {ECO:0000244|PDB:2UXT}.
FT STRAND 129 131 {ECO:0000244|PDB:2UXT}.
FT STRAND 136 143 {ECO:0000244|PDB:2UXT}.
FT TURN 146 148 {ECO:0000244|PDB:2UXT}.
FT HELIX 149 154 {ECO:0000244|PDB:2UXT}.
FT STRAND 158 164 {ECO:0000244|PDB:2UXT}.
FT HELIX 166 170 {ECO:0000244|PDB:2UXT}.
FT STRAND 171 173 {ECO:0000244|PDB:2UXT}.
FT TURN 177 179 {ECO:0000244|PDB:2UXT}.
FT STRAND 180 191 {ECO:0000244|PDB:2UXT}.
FT STRAND 203 205 {ECO:0000244|PDB:2UXT}.
FT STRAND 210 214 {ECO:0000244|PDB:2UXT}.
FT STRAND 217 219 {ECO:0000244|PDB:2UXT}.
FT STRAND 221 224 {ECO:0000244|PDB:2UXT}.
FT STRAND 226 235 {ECO:0000244|PDB:2UXT}.
FT STRAND 242 246 {ECO:0000244|PDB:2UXT}.
FT STRAND 252 256 {ECO:0000244|PDB:2UXT}.
FT STRAND 258 273 {ECO:0000244|PDB:2UXT}.
FT STRAND 278 284 {ECO:0000244|PDB:2UXT}.
FT STRAND 291 294 {ECO:0000244|PDB:2UXT}.
FT STRAND 319 325 {ECO:0000244|PDB:2UXT}.
FT STRAND 340 343 {ECO:0000244|PDB:2UXT}.
FT STRAND 351 358 {ECO:0000244|PDB:2UXT}.
FT STRAND 360 364 {ECO:0000244|PDB:2UXT}.
FT STRAND 376 379 {ECO:0000244|PDB:2UXT}.
FT STRAND 383 398 {ECO:0000244|PDB:2UXT}.
FT STRAND 402 408 {ECO:0000244|PDB:2UXT}.
FT HELIX 415 417 {ECO:0000244|PDB:2UXT}.
FT STRAND 421 435 {ECO:0000244|PDB:2UXT}.
FT STRAND 446 452 {ECO:0000244|PDB:2UXT}.
FT HELIX 453 457 {ECO:0000244|PDB:2UXT}.
FT STRAND 461 467 {ECO:0000244|PDB:2UXT}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 1 467 ihamap:FtsP [T]
FT MYHIT 1 27 iprf:TAT [T]
FT MYHIT 223 287 ipfam:Cu-oxidase [T]
FT MYHIT 52 166 ipfam:Cu-oxidase_3 [T]
FT MYHIT 359 468 ipfam:Cu-oxidase_2 [T]
SQ SEQUENCE 470 AA; 51858 MW; C843A5A4CB146688 CRC64;
MSLSRRQFIQ ASGIALCAGA VPLKASAAGQ QQPLPVPPLL ESRRGQPLFM TVQRAHWSFT
PGTRASVWGI NGRYLGPTIR VWKGDDVKLI YSNRLTENVS MTVAGLQVPG PLMGGPARMM
SPNADWAPVL PIRQNAATLW YHANTPNRTA QQVYNGLAGM WLVEDEVSKS LPIPNHYGVD
DFPVIIQDKR LDNFGTPEYN EPGSGGFVGD TLLVNGVQSP YVEVSRGWVR LRLLNASNSR
RYQLQMNDGR PLHVISGDQG FLPAPVSVKQ LSLAPGERRE ILVDMSNGDE VSITCGEAAS
IVDRIRGFFE PSSILVSTLV LTLRPTGLLP LVTDSLPMRL LPTEIMAGSP IRSRDISLGD
DPGINGQLWD VNRIDVTAQQ GTWERWTVRA DEPQAFHIEG VMFQIRNVNG AMPFPEDRGW
KDTVWVDGQV ELLVYFGQPS WAHFPFYFNS QTLEMADRGS IGQLLVNPVP
//
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