ID A0A4Y6PXU4_PERCE Unreviewed; 798 AA.
AC A0A4Y6PXU4; A0A5B8YEH2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN Name=pbpC {ECO:0000313|EMBL:QDG52817.1};
GN ORFNames=FIV42_19325 {ECO:0000313|EMBL:QDG52817.1};
OS Persicimonas caeni.
OC Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae;
OC Persicimonas.
OX NCBI_TaxID=2292766 {ECO:0000313|EMBL:QDG52817.1, ECO:0000313|Proteomes:UP000315995};
RN [1] {ECO:0000313|EMBL:QDG52817.1, ECO:0000313|Proteomes:UP000315995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YN101 {ECO:0000313|EMBL:QDG52817.1,
RC ECO:0000313|Proteomes:UP000315995};
RA Wang S.;
RT "Persicimonas caeni gen. nov., sp. nov., a predatory bacterium isolated
RT from solar saltern.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
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DR EMBL; CP041186; QDG52817.1; -; Genomic_DNA.
DR RefSeq; WP_141199278.1; NZ_CP041186.1.
DR AlphaFoldDB; A0A4Y6PXU4; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000315995; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:InterPro.
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; IPR050396; Glycosyltr_51/Transpeptidase.
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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000315995};
KW Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT DOMAIN 58..226
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 314..585
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 709..793
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 798 AA; 86523 MW; 20017FC47EF413E6 CRC64;
MKNSHKALTV ICTTALLAAG AALWLVPFPG ELLSYDNLTS TRLVDRHGRP LREALGATEG
RARAVGLDAI SPHMVAATVH AEDRRFWSHA GVDPLAVGRA AWQNVTNVEI VSGASTITQQ
VAKMVAGGSR ARTLPNKLEE MVLAVRLDKQ ETKRSILEQY LNRAPYGNQL FGVAAAASMY
FDKPPSQLTL AESALLAGIP RAPSLNNPYA DFERAKRVQR RVLALMHERG VIDDAAYRRA
LDEELTVVGR RGRVMAAHFT DHLLSERGPL SRLGKLGRPQ RIETTLDLDL QHKVRGIVGQ
ELSRLEKKNV GQAAVVVLDT KTAEVLAWVG SRDYFDAEGD GANDGVLARR QPGSALKPFV
YGLYLESGGT AADMLPDFPA QFPAADGVYI PENYDRSYHG PVSVRDALAS SLNIPAVHVT
HRLGAEAVHQ KLLALGLDTL DADADHYGLG LALGNGEVRL LDLAAAYAAL GRLGHPKPVQ
LTDQEPRTKN QEPKKRLLSA QTSYLLLDIL SDDRARSRGF GRYSALHLPY KVAAKTGTSA
GFRDNWAVGV TPDYTVAVWA GNFDATPMLG SSGVTGAAPI MRQVFQALYP DAASPADVDW
YEAPKGVEER TVCALSGQKP GHLCPSTRLE SFAGEASWAE LADCEIHRTF AIDTRNGLLA
GPDCPDAHVE EREFLDVPDD WTEWALERGH RLPPTQHSPL CGDDPGDAAR AADLRITHPM
PGDTFVLDPS LPRSEQQVAL RVEVPASRRD DTLTWFVDGE AVATVDAPFR AFWKLAPGEH
AVGVGRGRVE ASVTVRVE
//
