ID Q1I4E1_PSEE4 Unreviewed; 782 AA.
AC Q1I4E1;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpC {ECO:0000313|EMBL:CAK17495.1};
GN OrderedLocusNames=PSEEN4842 {ECO:0000313|EMBL:CAK17495.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK17495.1, ECO:0000313|Proteomes:UP000000658};
RN [1] {ECO:0000313|EMBL:CAK17495.1, ECO:0000313|Proteomes:UP000000658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48 {ECO:0000313|EMBL:CAK17495.1,
RC ECO:0000313|Proteomes:UP000000658};
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CT573326; CAK17495.1; -; Genomic_DNA.
DR RefSeq; WP_011535857.1; NC_008027.1.
DR AlphaFoldDB; Q1I4E1; -.
DR STRING; 384676.PSEEN4842; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR GeneID; 32807798; -.
DR KEGG; pen:PSEEN4842; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_3_6; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000658; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 62..228
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 335..419
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 696..778
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 782 AA; 85955 MW; A7CEDDD892E93335 CRC64;
MPSLARPRLA RGLRRVCVTI LSTFALLWLA DRIWPLPMPG DDLARVVLAE DGTPLWRFAD
ADGVWRYPVS PDEVSPLYLE ALLAYEDRWF YQHPGVNPMA LARAAWLNVR GGRVVSGGST
LSMQVARLLD PHDRTLAGKL RQLWRTAQLE WHLSKQEILQ LYLNRAPFGG TLQGVAAASW
AYLGKSPKHL TPAEAALLAV LPQAPSRLRP DRHPERAQRA RDKVLQRLAE YQVWPAQRID
EAREEPLLLA PRQEPALAPL LARRLNSPDS PPLIRTTIDA ALQRRLEDLL LGWRARLPER
TSAALLVVET QSMAVRAYLG SIDLADERRF GHVDMIHALR SPGSTLKPFL YAMAMDEGLI
HSESLLQDVP RRYGDYRPGN FSMGFSGPVS ASSALALSLN LPAVQLLEAY GPKRFAAQMR
MGGVPLILPP LAEPNLSLIL GGAGSRLEDL VGGYAAFARE GRSAQIRLQP QDPLLERRLL
SPGSAWITRR ILSGLARPDR DPHAELVQRP QLAWKTGTSY GFRDAWSVGV GPRYLIGVWI
GRPDGTPVPG QFGLASAAPL MLQVHDLLSN RDAQRGINVP VEPVPESVGV AAICWPLGQP
MNRQDPNCRR QRFAWTLDGT TPPTLQAADQ PLGLGLHESV WVNEQGLRVG SGCPGATARD
IALWPAPLEP WLPRAERRLV RLPAVDPTCP PLVGASAPPL SIVGVRPGDN LRRPATSSEA
LQLRVSALGG GGQRWWFLNG QPLGETRGQD SLLVRFEQVG RTELSALDES GETARVEFQV
SE
//
