ID A0A853G145_9BURK Unreviewed; 717 AA.
AC A0A853G145;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
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:NYT50988.1};
GN ORFNames=H0A72_16880 {ECO:0000313|EMBL:NYT50988.1};
OS Parapusillimonas granuli.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Alcaligenaceae; Parapusillimonas.
OX NCBI_TaxID=380911 {ECO:0000313|EMBL:NYT50988.1, ECO:0000313|Proteomes:UP000559809};
RN [1] {ECO:0000313|EMBL:NYT50988.1, ECO:0000313|Proteomes:UP000559809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24012 {ECO:0000313|EMBL:NYT50988.1,
RC ECO:0000313|Proteomes:UP000559809};
RA Szabo A., Felfoldi T.;
RT "Taxonomic revisions and descriptions of new bacterial species based on
RT genomic comparisons in the high-G+C-content subgroup of the family
RT Alcaligenaceae.";
RL Submitted (JUL-2020) 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};
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NYT50988.1}.
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DR EMBL; JACCEM010000009; NYT50988.1; -; Genomic_DNA.
DR RefSeq; WP_180157452.1; NZ_JACCEM010000009.1.
DR AlphaFoldDB; A0A853G145; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000559809; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000559809};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..717
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032322387"
FT DOMAIN 53..206
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 304..569
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 621..708
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 717 AA; 76496 MW; 7C4C13463F0DBF49 CRC64;
MKRMPAWVLA LAACFCGASW AGISYQDVRD GYHASDAVVL DRAGRTVQRL RADFRERRGD
WVALQDISPA LQRAVILSED RRFHDHAGVD WTAVWSAAWG NLVSGGRRGA STLSMQLLGF
IDDQYRRGPG GRGIMQKLGQ AYAALELEAE WSKSQILEAY LNLAAFRGEL VGVDALARAL
FRKAPSGLET REAALAAVLL RGPNAPQAVL VRRACGLLAE MGSPEECSGL GDFVQLTLDH
RPARWADGAG LAPHFARLAL NGAGAAGPGA RIATTLDADL QRHALAVIER NLLALGDANV
SDAALVVLDN ETGGVLAYVG SSGDLSGAAQ VDHARALRQA GSTLKPFLYA LAIEQERLTA
VSLLDDGPLD LPTGNGLYIP QNYDKRFSGW VSVRGALGSS LNIPAVRALM MVTPEAFARR
LAALGLPLDR SGDYYGYSLA LGSADVSLLS LTNAYRALAR GGVHSEPRYV VDGAGAAGSR
RVAAEGAAWI VGDILADRQA RARTFGFDSP LSTPFWTAVK TGTSKDMRDN WCVGWSSRYT
VGVWVGNSTG VSMREVSGVS GAGPVWHEIM AYLHRHEASV QPPAPAAVRP AQVVFQDGLE
PARKDYFLGD TAITQVRLAR AQGAEGAAPL RIAAPADGTI LALDPDIPLA RQRSVFSVSG
PGRGRADGLA WRVDGRLVGR GDRLEWQPEP GTHRVQLIDE HGRLRDEVGI QVRAGGR
//
