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 26-FEB-2020, entry version 107.
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., 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}.
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_SDVX01000001.1.
DR SMR; P0AD69; -.
DR STRING; 155864.EDL933_0087; -.
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; CLU_009289_6_2_6; -.
DR KO; K03587; -.
DR BioCyc; ECOO157:FTSI-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
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:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
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; 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
//
