ID A0A0H3B7X1_YERPY Unreviewed; 587 AA.
AC A0A0H3B7X1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
DE Flags: Precursor;
GN Name=ftsI {ECO:0000256|HAMAP-Rule:MF_02080};
GN OrderedLocusNames=YPK_3524 {ECO:0000313|EMBL:ACA69791.1};
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800 {ECO:0000313|EMBL:ACA69791.1};
RN [1] {ECO:0000313|EMBL:ACA69791.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YPIII {ECO:0000313|EMBL:ACA69791.1};
RG US DOE Joint Genome Institute;
RA Challacombe J.F., Bruce D., Detter J.C., Green L., Land M., Munk C.,
RA Lindler L.E., Nikolich M.P., Brettin T.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000950; ACA69791.1; -; Genomic_DNA.
DR RefSeq; WP_011191731.1; NZ_CP009792.1.
DR AlphaFoldDB; A0A0H3B7X1; -.
DR GeneID; 66842897; -.
DR KEGG; ypy:YPK_3524; -.
DR PATRIC; fig|502800.11.peg.4267; -.
DR UniPathway; UPA00219; -.
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 Glycosyltransferase {ECO:0000313|EMBL:ACA69791.1};
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 Transferase {ECO:0000313|EMBL:ACA69791.1};
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 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT DOMAIN 67..219
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 259..553
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 306
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 587 AA; 63658 MW; 3B68E61E48A9431E CRC64;
MKTARPGKLK RQEEQASFIS WRFALLCGCI LLALVGLIMR TAYLQVINPD KLVREGDMRS
LRVQEVPTAR GMISDRSGRP LAVSVPVNAV WADPKELIEQ GGISLDTRWK ALSDALEIPL
DQLATRINAN PKGRFVYLAR QVNPAIGDYI RKLKLPGIHL RQESRRYYPA GQVMAHIIGV
TNIDGQGIEG VEKSFDRWLT GQPGERTVRK DRYGRVIEDI SSVDSQAAHN LVLSVDERLQ
ALVYRELNNA VAFNKAESGT AVLVDVNTGE VLAMANSPSY NPNNLTGTPK DAMRNRAITD
IFEPGSTVKP MVVMTALQHG VVKENSVLNT LPYFVNGHQI KDVARYAELS VTGILQKSSN
VGVSKLALAM PSSALVDTYS RFGFGKATNL GLVGESSGLY PKKQRWSDIE RATFSFGYGL
MVTPLQLARV YATIGSMGVY RPLSITRVDP PVAGERIFPE PLVRTVVHMM ESVALPGGGG
TKAAIKGYRI AIKTGTAKKV GPDGKYMDRY LAYTAGVAPA SNPRFALVVV INDPQAGKYY
GGAVSAPVFG AIMGGVLRTM NIEPDALPTG DKSELVINTK EGSGGRS
//
