ID M4TSJ6_9XANT Unreviewed; 622 AA.
AC M4TSJ6;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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 ORFNames=XAC29_03950 {ECO:0000313|EMBL:AGH76316.1};
OS Xanthomonas axonopodis Xac29-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1304892 {ECO:0000313|EMBL:AGH76316.1, ECO:0000313|Proteomes:UP000011979};
RN [1] {ECO:0000313|EMBL:AGH76316.1, ECO:0000313|Proteomes:UP000011979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xac29-1 {ECO:0000313|EMBL:AGH76316.1,
RC ECO:0000313|Proteomes:UP000011979};
RA Chen G., Zou H., Ye G., Song X., Ji Z., Ma W.;
RT "Completed genome of Xanthomonas axonopodis sp. Xac29-1.";
RL Submitted (MAR-2013) 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 -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02080}.
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DR EMBL; CP004399; AGH76316.1; -; Genomic_DNA.
DR RefSeq; WP_003485291.1; NC_020800.1.
DR AlphaFoldDB; M4TSJ6; -.
DR GeneID; 66909968; -.
DR KEGG; xao:XAC29_03950; -.
DR PATRIC; fig|1304892.4.peg.869; -.
DR HOGENOM; CLU_009289_6_2_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000011979; Chromosome.
DR GO; GO:0005886; C: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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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 DOMAIN 61..209
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 250..546
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 571..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 297
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 622 AA; 66871 MW; 9D0E59B2582D0B27 CRC64;
MKAGRNRPRS NFNLRGRLTL VGIALGLCSV TLIGRAAYVQ LVNRDFYQRQ GEARYLRELP
IATSRGMITD RNGEPLAVST PVESIWVNPQ ELLRNPDRIP ELAKALGQPL DDLNAKLAQK
AGKEFMYLQR RINPDKAHAI VDLKIPGVFS QREFRRFYPQ GEAMAHVLGF TNIDDRGQEG
LELAFDEWLR GKPGSKKVVR DARGAIVESV DLVRPAQPGK DLTLSIDRRI QFLAYKELRN
ALVENNAAGG SMVVMDVATG EVLAMVNLPT YNPNSVTGIN PSARRNRAVT DLVEPGSTMK
PLTVATALTA GVVTKDTVID TNPGYMSVGR FTIRDVPRNN GVLNVTGVIT RSSNIGAAKI
AAKVPDQTFY QSIRNFGYGS APHSGFPGES AGVVLQPARW SGPSKTTMSY GYGLSVTPLQ
IAQAYATLGN GGKLTPPTFV RGQHNETRQV ITPEVARQVI DMMETVVTQG GAKGAAILGY
HVAGKTGTAR KNGANGYERG HYNALFAGLV PATRPRFATV IVINDPQGKV YYGGLVSAPV
FHRVMEGALR LMDVPPDDIQ SWLAAQAAGK TGQPVVKPQS VDPDPALVPD PVDEVSAGIP
TALAPAPAAA PAQPAPLQES RQ
//
