ID A0A089ZPX2_9PSED Unreviewed; 582 AA.
AC A0A089ZPX2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=LT40_04070 {ECO:0000313|EMBL:AIS16626.1};
OS Pseudomonas rhizosphaerae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS16626.1, ECO:0000313|Proteomes:UP000029499};
RN [1] {ECO:0000313|EMBL:AIS16626.1, ECO:0000313|Proteomes:UP000029499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS16626.1};
RX PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA Kwak Y., Jung B.K., Shin J.H.;
RT "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL J. Biotechnol. 193:137-138(2015).
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; CP009533; AIS16626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A089ZPX2; -.
DR STRING; 216142.LT40_04070; -.
DR KEGG; prh:LT40_04070; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_2_6; -.
DR OrthoDB; 9789078at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000029499; 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 ECO:0000313|EMBL:AIS16626.1};
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|ARBA:ARBA00022801, 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 Reference proteome {ECO:0000313|Proteomes:UP000029499};
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 55..204
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 245..545
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 558..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 582 AA; 63371 MW; 59DD5BEB997C1771 CRC64;
MMKLDGALFP WRFRLMVGLL LLLVGGIVAQ IVYLQVINRD FLIGQGDARS MRHIPIPAHR
GLITDRNGEP LAVSTPVTTL WANPKEMQLA KDKWPALARA LGQDPKALAE RLEAQASKEF
IYLVRGLTPE QGASVLDLKT PGVYGIEEFR RFYPAGDVTA HMVGFTDLDD HGREGVELAY
DEWLAGVPGK RQVIKDRRGR LIKDVQVTKN AKAGKTLALS IDLRLQYLAS RELRNAITEN
EAKAGSMVIM DVKTGEVLAM VNQPTYNPNN RRTMLPAAMR NRAIIDVFEP GSTMKPISMS
AALESGRWKP TDKVEVYPGT LQIGRYTIKD VTKTEGPVLD LTGILINSSN VGMSKVAFDI
GGESIYRVMS AVGLGQYTGL GFPGERVGNL PNHREWRKAE TATLSYGYGL SVTALQLVHA
YAAIANNGRI VPLTILKSDQ PPTAAQVIPE KVAKTVQGML QQVIEDTRGV YRARVPSYHV
AGKSGTARKA TIGSRGYTEN AYRSLFAGFG PMSDPRYAIV VVIDEPSKGG YYGGLVSAPV
FSKVMSGTLR LMNVQPDNLP PPVPQQQVNA APATPLIKGG RG
//
