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Database: UniProt/SWISS-PROT
Entry: FTSI_ECO57
LinkDB: FTSI_ECO57
Original site: FTSI_ECO57 
ID   FTSI_ECO57              Reviewed;         588 AA.
AC   P0AD69; P04286;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   23-MAY-2018, entry version 97.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase FtsI {ECO:0000255|HAMAP-Rule:MF_02080};
DE            EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02080};
DE   AltName: Full=Penicillin-binding protein 3 {ECO:0000255|HAMAP-Rule:MF_02080};
DE            Short=PBP-3 {ECO:0000255|HAMAP-Rule:MF_02080};
DE   Flags: Precursor;
GN   Name=ftsI {ECO:0000255|HAMAP-Rule:MF_02080}; Synonyms=pbpB;
GN   OrderedLocusNames=Z0094, ECs0088;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall
CC       at the division septum. {ECO:0000255|HAMAP-Rule:MF_02080}.
CC   -!- CATALYTIC ACTIVITY: Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-
CC       D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are
CC       N-acyl substituents of D-alanine. {ECO:0000255|HAMAP-
CC       Rule:MF_02080}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02080}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02080}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02080}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02080}.
DR   EMBL; AE005174; AAG54388.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33511.1; -; Genomic_DNA.
DR   PIR; H85490; H85490.
DR   PIR; H90639; H90639.
DR   RefSeq; NP_308115.1; NC_002695.1.
DR   RefSeq; WP_000642196.1; NZ_NOKN01000002.1.
DR   ProteinModelPortal; P0AD69; -.
DR   SMR; P0AD69; -.
DR   STRING; 155864.Z0094; -.
DR   DrugBank; DB05659; faropenem medoxomil.
DR   PRIDE; P0AD69; -.
DR   EnsemblBacteria; AAG54388; AAG54388; Z0094.
DR   EnsemblBacteria; BAB33511; BAB33511; BAB33511.
DR   GeneID; 913535; -.
DR   KEGG; ece:Z0094; -.
DR   KEGG; ecs:ECs0088; -.
DR   PATRIC; fig|386585.9.peg.188; -.
DR   eggNOG; ENOG4105CJN; Bacteria.
DR   eggNOG; COG0768; LUCA.
DR   HOGENOM; HOG000049554; -.
DR   KO; K03587; -.
DR   OMA; NVGMIKI; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_02080; FtsI_transpept; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR037532; FtsI_transpept.
DR   InterPro; IPR005311; PBP_dimer.
DR   InterPro; IPR036138; PBP_dimer_sf.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Cell cycle; Cell division; Cell inner membrane;
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW   Complete proteome; Hydrolase; Membrane; Peptidoglycan synthesis;
KW   Protease; Reference proteome; Septation; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    577       Peptidoglycan D,D-transpeptidase FtsI.
FT                                /FTId=PRO_0000043363.
FT   PROPEP      578    588       {ECO:0000250|UniProtKB:P0AD68}.
FT                                /FTId=PRO_0000043364.
FT   TRANSMEM     19     39       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_02080}.
FT   ACT_SITE    307    307       Acyl-ester intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_02080}.
SQ   SEQUENCE   588 AA;  63877 MW;  C89A403D5980B2CD CRC64;
     MKAAAKTQKP KRQEEHANFI SWRFALLCGC ILLALAFLLG RVAWLQVISP DMLVKEGDMR
     SLRVQQVSTS RGMITDRSGR PLAVSVPVKA IWADPKEVHD AGGISVGDRW KALANALNIP
     LDQLSARINA NPKGRFIYLA RQVNPDMADY IKKLKLPGIH LREESRRYYP SGEVTAHLIG
     FTNVDSQGIE GVEKSFDKWL TGQPGERIVR KDRYGRVIED ISSTDSQAAH NLALSIDERL
     QALVYRELNN AVAFNKAESG SAVLVDVNTG EVLAMANSPS YNPNNLSGTP KEAMRNRTIT
     DVFEPGSTVK PMVVMTALQR GVVRENSVLN TIPYRINGHE IKDVARYSEL TLTGVLQKSS
     NVGVSKLALA MPSSALVDTY SRFGLGKATN LGLVGERSGL YPQKQRWSDI ERATFSFGYG
     LMVTPLQLAR VYATIGSYGI YRPLSITKVD PPVPGERVFP ESIVRTVVHM MESVALPGGG
     GVKAAIKGYR IAIKTGTAKK VGPDGRYINK YIAYTAGVAP ASQPRFALVV VINDPQAGKY
     YGGAVSAPVF GAIMGGVLRT MNIEPDALTT GDKNEFVINQ GEGTGGRS
//
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