ID A0A0H3MCS6_ECO7I Unreviewed; 588 AA.
AC A0A0H3MCS6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Peptidoglycan D,D-transpeptidase FtsI {ECO:0000256|HAMAP-Rule:MF_02080};
DE EC=3.4.16.4 {ECO:0000256|HAMAP-Rule:MF_02080};
DE AltName: Full=Penicillin-binding protein 3 {ECO:0000256|HAMAP-Rule:MF_02080};
DE Short=PBP-3 {ECO:0000256|HAMAP-Rule:MF_02080};
GN Name=ftsI {ECO:0000256|HAMAP-Rule:MF_02080,
GN ECO:0000313|EMBL:CAR16228.1};
GN OrderedLocusNames=ECIAI39_0087 {ECO:0000313|EMBL:CAR16228.1};
OS Escherichia coli O7:K1 (strain IAI39 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585057 {ECO:0000313|EMBL:CAR16228.1, ECO:0000313|Proteomes:UP000000749};
RN [1] {ECO:0000313|Proteomes:UP000000749}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI39 / ExPEC {ECO:0000313|Proteomes:UP000000749};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC division septum. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_02080};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02080}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02080}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02080}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02080}.
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DR EMBL; CU928164; CAR16228.1; -; Genomic_DNA.
DR RefSeq; WP_000642212.1; NC_011750.1.
DR RefSeq; YP_002406136.1; NC_011750.1.
DR AlphaFoldDB; A0A0H3MCS6; -.
DR STRING; 585057.ECIAI39_0087; -.
DR KEGG; ect:ECIAI39_0087; -.
DR PATRIC; fig|585057.6.peg.96; -.
DR HOGENOM; CLU_009289_6_2_6; -.
DR OMA; QDNYSLA; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000749; 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: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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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; 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 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 {ECO:0000256|ARBA:ARBA00022645, ECO:0000256|HAMAP-
KW Rule:MF_02080}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02080};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02080};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02080};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02080};
KW Protease {ECO:0000256|HAMAP-Rule:MF_02080};
KW Septation {ECO:0000256|HAMAP-Rule:MF_02080};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02080};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02080}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT DOMAIN 69..220
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 260..554
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 307
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 588 AA; 63877 MW; 89D6BED34836F77D CRC64;
MKAAAKTQKP KRQEEHANFI SWRFALLCGC ILLALAFLLG RVAWLQVISP DMLVKEGDMR
SLRVQQVSTS RGMITDRSGR PLAVSVPVKA IWADPKEVHD AGGISVGDRW KALANALNIP
LDQLSARINA NPKGRFIYLA RQVNPDMAEY IKKLKLPGIH LREESRRYYP SGEVTAHLIG
FTNVDSQGIE GVEKSFDKWL TGQPGERIVR KDRYGRVIED ISSTDSQAAH NLALSIDERL
QALVYRELNN AVAFNKAESG SAVLVDVNTG EVLAMANSPS YNPNNLSGTP KEAMRNRTIT
DVFEPGSTVK PMVVMTALQR GVVRENSVLN TVPYRINGHE 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
//