ID A0A839GHV1_9BACT Unreviewed; 784 AA.
AC A0A839GHV1;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN ORFNames=FHS90_003969 {ECO:0000313|EMBL:MBA9079234.1};
OS Rufibacter quisquiliarum.
OC Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC Hymenobacteraceae; Rufibacter.
OX NCBI_TaxID=1549639 {ECO:0000313|EMBL:MBA9079234.1, ECO:0000313|Proteomes:UP000563094};
RN [1] {ECO:0000313|EMBL:MBA9079234.1, ECO:0000313|Proteomes:UP000563094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29854 {ECO:0000313|EMBL:MBA9079234.1,
RC ECO:0000313|Proteomes:UP000563094};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-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:MBA9079234.1}.
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DR EMBL; JACJIQ010000019; MBA9079234.1; -; Genomic_DNA.
DR RefSeq; WP_182514187.1; NZ_JACJIQ010000019.1.
DR AlphaFoldDB; A0A839GHV1; -.
DR Proteomes; UP000563094; Unassembled WGS sequence.
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 ECO:0000313|EMBL:MBA9079234.1}; 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:UP000563094};
KW Transferase {ECO:0000313|EMBL:MBA9079234.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..228
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 316..555
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 696..777
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 784 AA; 87924 MW; A0AB3FA147A91ABD CRC64;
MPLLQAFTRS PKLPLSNRGR RWLCAAVATG VVTFCLYSLL NLLFPLKISI AYSPVITAAD
GSVLNAFLSP DDKWRMQLEP GEVSPSLKKA ILLKEDKYFY YHFGVNPVAL TRAFLNNLTH
GRTTSGASTI TMQVARLLYP KERTYANKLV DMFRAIQLEL TYSKDEILLL YLNLVPYGGN
IEGVKAASVL YFQQSPQQLS LAQAVTLTVI PNKPSSLRIG RQNERIVAFR DKWLAYYLKE
KAFPKESIED ARQEPLEAFR LEAPKIAPHY AYRLHRQYPQ QPIIKSTLNR QVQDKVQQLA
YNYLQRLKGY NIHNAAVLVV NNQTKAVEAY LGSADFNDGL HGGQVDGVKA IRSPGSTLKP
FLYATAFDRG LITPKTIITD VPIDYAGYRP ENYYGDYNGY ITIERALATS LNIPAVKLLD
QVGVQAFVQK LKQAEFSQMK KHGGSLGLSL ILGGCGVKLE ELTALYSSFA NQGTYASLRW
LQGQKDTLST PLLSPAATFM LNEILTQLQR PDLPHNSQNS AHLPKIAWKT GTSYGRKDAW
SIGYNKKYTV GVWVGNFSGQ GVPELNGTDT ATPLLFDIFN TIDYNSPESW FRAPNGISYR
DVCAVTGLPA NSFCQDQIMD TYIPSVSSMA KCTHLKKVAV SLDGKYAYCT SCLPETGYHH
QWYPNHAPEM LTFFVNQHLP YVSLPPHNPS CSRIFQEYAP IISSPTANME YLLEASDHQK
LMLQCNAHNE VKKVYWYLND QFLQSAPANQ PVFFEPPQAG KLKISCLDDQ GRNTNIQVTV
RFMD
//
