ID A0A369QHN8_9BACT Unreviewed; 379 AA.
AC A0A369QHN8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:RDC61808.1};
GN ORFNames=AHMF7616_00397 {ECO:0000313|EMBL:RDC61808.1};
OS Adhaeribacter pallidiroseus.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Adhaeribacter.
OX NCBI_TaxID=2072847 {ECO:0000313|EMBL:RDC61808.1, ECO:0000313|Proteomes:UP000253919};
RN [1] {ECO:0000313|EMBL:RDC61808.1, ECO:0000313|Proteomes:UP000253919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF7616 {ECO:0000313|EMBL:RDC61808.1,
RC ECO:0000313|Proteomes:UP000253919};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Adhaeribacter sp. HMF7616 genome sequencing and assembly.";
RL Submitted (APR-2018) 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=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
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:RDC61808.1}.
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DR EMBL; QASA01000001; RDC61808.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369QHN8; -.
DR Proteomes; UP000253919; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:RHEA.
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; IPR036950; PBP_transglycosylase.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF00912; Transgly; 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:0000313|EMBL:RDC61808.1};
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:UP000253919};
KW Transferase {ECO:0000313|EMBL:RDC61808.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..229
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
SQ SEQUENCE 379 AA; 42737 MW; A7248DB791AF4F6B CRC64;
MWRQRITRLI TFNRSYQSCT KFKKTTVGGV LIVALLGLLL VFLNFWFPLR VQITYSPVIT
ASDGSVINAF LSPDDKWRMQ LQTHEINPLL KKAILLKEDR YFYYHPGVNP VALSRALVNN
VIAGKTTSGA STITMQVARL LYPRQRTIPN KLKELFRALK LELNYSKDEI LTLYLNLVPF
GGNIEGIKAA SVLYFQQSPQ ELSLAQAVTL TVIPNKPSSL RIGMKNDRIV SFRNKWLWYF
AKQKAFPAKE IADAINEPLV AYRSEAPQIA PHFAYRLQKQ FPNQAIIQTN LNRAIQEKVA
QLAYNYQGTL RARNIRNASV LVINNQTKAV EAYLGSADFS DHEHGGQVDG VRANRSPGST
LKPLLYALAF DKGLITPAP
//
