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   04-NOV-2026, entry version 133.
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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; 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., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   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., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   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 at the
CC       division septum. {ECO:0000255|HAMAP-Rule:MF_02080}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC         transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC         substituents of D-alanine.; EC=3.4.16.4; Evidence={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}.
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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_002695.2.
DR   RefSeq; WP_000642196.1; NZ_AP018488.1.
DR   AlphaFoldDB; P0AD69; -.
DR   SMR; P0AD69; -.
DR   STRING; 155864.Z0094; -.
DR   DrugBank; DB05659; Faropenem medoxomil.
DR   GeneID; 75202099; -.
DR   GeneID; 913535; -.
DR   KEGG; ece:Z0094; -.
DR   KEGG; ecs:ECs_0088; -.
DR   PATRIC; fig|386585.9.peg.188; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_6_2_6; -.
DR   OMA; AADQYSD; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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-UniRule.
DR   GO; GO:0071555; P:cell wall organization; IEA:TreeGrafter.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   FunFam; 3.40.710.10:FF:000003; Peptidoglycan D,D-transpeptidase FtsI; 1.
DR   FunFam; 3.90.1310.10:FF:000003; Peptidoglycan D,D-transpeptidase FtsI; 1.
DR   Gene3D; 1.10.150.770; -; 1.
DR   Gene3D; 3.30.450.330; -; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   HAMAP; MF_02080; FtsI_transpept; 1.
DR   InterPro; IPR050515; Beta-lactam/transpept.
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   NCBIfam; NF011685; ftsI; 1.
DR   PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Cell cycle; Cell division; Cell inner membrane;
KW   Cell membrane; Cell shape; Cell wall biogenesis/degradation; Hydrolase;
KW   Membrane; Peptidoglycan synthesis; Protease; Reference proteome; Septation;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..577
FT                   /note="Peptidoglycan D,D-transpeptidase FtsI"
FT                   /id="PRO_0000043363"
FT   PROPEP          578..588
FT                   /evidence="ECO:0000250|UniProtKB:P0AD68"
FT                   /id="PRO_0000043364"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT   ACT_SITE        307
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="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
//