FTSP_ECOLI
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 03-AUG-2022, entry version 162.
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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
RX PubMed=1557036; DOI=10.1007/bf00280009;
RA Coleman J.;
RT "Characterization of the Escherichia coli gene for 1-acyl-sn-glycerol-3-
RT 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 in the
RT 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 and
RT 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 for its
RT 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., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 28-470, AND SUBCELLULAR 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 SufI
RT (FtsP) localizes to the septal ring and has a multicopper oxidase-like
RT 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 the
CC divisomal assembly under conditions of stress. {ECO:0000255|HAMAP-
CC 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 peptide
CC cleavage has been experimentally proven. Can also be exported by the
CC Sec system.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are sensitive to
CC oxidative stress and DNA damage at high temperature. They also exhibit
CC filamentation. {ECO:0000269|PubMed:17766410}.
CC -!- MISCELLANEOUS: Is used as a model substrate in studies of the twin-
CC 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_SSZK01000023.1.
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 AlphaFoldDB; P26648; -.
DR SMR; P26648; -.
DR BioGRID; 4260932; 62.
DR BioGRID; 849379; 3.
DR DIP; DIP-10942N; -.
DR IntAct; P26648; 9.
DR STRING; 511145.b3017; -.
DR jPOST; P26648; -.
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; fig|1411691.4.peg.3713; -.
DR EchoBASE; EB1350; -.
DR eggNOG; COG2132; Bacteria.
DR HOGENOM; CLU_009100_2_4_6; -.
DR InParanoid; P26648; -.
DR OMA; GMWIIED; -.
DR PhylomeDB; P26648; -.
DR BioCyc; EcoCyc:EG11376-MON; -.
DR EvolutionaryTrace; P26648; -.
DR PRO; PR:P26648; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IDA:EcoCyc.
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; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IMP:CACAO.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:EcoCyc.
DR GO; GO:0006979; P:response to oxidative stress; IMP:EcoCyc.
DR Gene3D; 2.60.40.420; -; 3.
DR HAMAP; MF_00915; FtsP; 1.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR026589; FtsP.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR PANTHER; PTHR11709; PTHR11709; 1.
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; Direct protein sequencing;
KW Periplasm; Reference proteome; Signal.
FT SIGNAL 1..27
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00915,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 28..470
FT /note="Cell division protein FtsP"
FT /id="PRO_0000002993"
FT DOMAIN 68..164
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00915"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2UXV"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:2UXT"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:2UXT"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2UXT"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:2UXT"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:2UXT"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:2UXT"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2UXT"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 180..191
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 258..273
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 351..358
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 383..398
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 402..408
FT /evidence="ECO:0007829|PDB:2UXT"
FT HELIX 415..417
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 421..435
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:2UXT"
FT HELIX 453..457
FT /evidence="ECO:0007829|PDB:2UXT"
FT STRAND 461..467
FT /evidence="ECO:0007829|PDB:2UXT"
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
