ID A0A8A4TSU2_SULCO Unreviewed; 811 AA.
AC A0A8A4TSU2;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 18-JUN-2025, entry version 15.
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:QTD52573.1};
GN ORFNames=J3U87_08875 {ECO:0000313|EMBL:QTD52573.1};
OS Sulfidibacter corallicola.
OC Bacteria; Pseudomonadati; Acidobacteriota; Holophagae;
OC Acanthopleuribacterales; Acanthopleuribacteraceae; Sulfidibacter.
OX NCBI_TaxID=2818388 {ECO:0000313|EMBL:QTD52573.1, ECO:0000313|Proteomes:UP000663929};
RN [1] {ECO:0000313|EMBL:QTD52573.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M133 {ECO:0000313|EMBL:QTD52573.1};
RA Wang G.;
RT "Acanthopleuribacteraceae sp. M133.";
RL Submitted (MAR-2021) 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}.
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DR EMBL; CP071793; QTD52573.1; -; Genomic_DNA.
DR RefSeq; WP_237382679.1; NZ_CP071793.1.
DR KEGG; scor:J3U87_08875; -.
DR Proteomes; UP000663929; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:InterPro.
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|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000663929};
KW Transferase {ECO:0000256|ARBA:ARBA00022676};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..236
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 314..443
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 719..801
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 811 AA; 90675 MW; 2659C9807C6735A6 CRC64;
MPFRVPLPSP VSGIRRCRNH PRKIAALVVL LLAGLVWFYQ ALPDPLFDDP TATVIEDRDG
RLLAARIAAD QQWRFPARDR VPDKFSRALI CFEDKRFHRH PGVDPLALVR AIVQNLRAGR
VESGASTLTM QVIRLSRKGQ PRTLWEKAVE ATLALRLECS AHKDRILALY AGHAPFGGNV
VGLDAAAWRY FGRRADNLSW AEAATLAVLP NNPALIHPGR NRDRLRAKRD RLLHRLHETG
AFDALTLELA KAEGLPPAPF PLPMQASHLL HRVHAEYPRG KRVRTTLDGK LQGQAIEILA
RFHRRLVTNG VHNGAALVLD NRTGRVLAYV GNTNRQDTLV GDGEDHGHAV DIVPAARSTG
SLLKPFLFAT ALDEGLILPQ SLLPDIPTNY GSYQPQNFDH AYRGAVPADL ALARSLNIPA
VRLQERLGTV RLHHQLKRMG LTHLTRAPSH YGLALILGGA ESSMWELAGR YAGLARTLNS
YGASGTYRAD DFAPPEIEVV QAEPELEGSS ARAPYLSAGA IWHTLEALTK VDRPDSQGLW
QYFTSARRIA WKTGTSFGFR DAWAIGVTPD HTVAVWVGNA DGEGRPGLTG VTTAAPIMFE
LFAKLPRGQH WFSRPDGDLN PVAVCVQSGD RAGMHCPETR ERQVPRAGLR VRACRYHQLV
HLDAEGRYRV HGDCASPSDM QHRAWFVLPP GQEWFFKRHN PSYRVLPPFH ERCKSGVTER
KNAMELIYPR ETTKIYIPRE LDGQLGKAVF EVAHRHPDTR IFWHLDDRFL GMTHHFHQMA
LQPKKGKHRL VLVDEAGERL ERSFEVTSDH H
//
