ID A0A840MUD7_9PROT Unreviewed; 695 AA.
AC A0A840MUD7;
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 ORFNames=HNQ59_003294 {ECO:0000313|EMBL:MBB5019986.1};
OS Chitinivorax tropicus.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Chitinivorax.
OX NCBI_TaxID=714531 {ECO:0000313|EMBL:MBB5019986.1, ECO:0000313|Proteomes:UP000575898};
RN [1] {ECO:0000313|EMBL:MBB5019986.1, ECO:0000313|Proteomes:UP000575898}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27165 {ECO:0000313|EMBL:MBB5019986.1,
RC ECO:0000313|Proteomes:UP000575898};
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:MBB5019986.1}.
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DR EMBL; JACHHY010000022; MBB5019986.1; -; Genomic_DNA.
DR RefSeq; WP_184041399.1; NZ_JACHHY010000022.1.
DR AlphaFoldDB; A0A840MUD7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000575898; 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 ECO:0000313|EMBL:MBB5019986.1}; 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:UP000575898};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:MBB5019986.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..695
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032407144"
FT DOMAIN 56..221
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 300..518
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 615..672
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 695 AA; 75467 MW; 08776705A8D40F8F CRC64;
MISLQRPLLL LCTLLSTSSA FALPAFQAVR QGWQPSESWL LDRRGAILAS KRINPHVRRL
EWVSLPDISP ELKKAVILSE DRRFLEHSGI DWQALAGAAK EQAEGGNRGA STLTMQLAGL
LDEDLKAGPD GRSLLQKLGQ IRAAKALEAD WSKDQILEGY LNLAPFRGEA IGVAAASTLL
FGKMPAGLNQ GESIILAVLL RGPNASADTI SRRACELANA MQARVGCAYL QGLASQALSL
ANKNRLAIND APEVAQRLLD QAGRSVKSTL DADLQRAVRE ILHRQLADLQ RQNTHNAAGL
VIDNRSGQVL AYVSENLDRS QVDGVQAKRQ AGSTLKPFLY QMAFAQRLLT PASLLDDSPV
NIDTAGGLYM PQNYDKSFRG TVSVRTSLAG SLNLPAIRTL LLVGIEPFYK HLNALGLDLP
QSADFYGFSL ALGSADVSLW QLTNAYRTLA NQGQASTPTL IPGNRPRGVQ VSDGAASWLV
GDILSDRGAR ASSFGLENPL ATRVWSAVKT GTSKDMRDNW CIGFTSRYTI GVWVGNFSGE
PMWNVSGVSG AAPAWREVVH RLHANQPSQP VAPPKGIVRQ MVKFTPAVEP PRREVFLAGT
ETAVIEQTST VGNPILYPTD GEIIALDPDI PVNRQRVRFE ADTTGQWLLN GKPLGQPASA
IWWQPLPGQY RLGFKGGLQP EKTIRFEVRG TLRRQ
//
