ID A0A0T5PFC7_9RHOB Unreviewed; 725 AA.
AC A0A0T5PFC7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbpG_1 {ECO:0000313|EMBL:QEW28923.1};
GN ORFNames=RIdsm_04764 {ECO:0000313|EMBL:QEW28923.1}, XM52_02515
GN {ECO:0000313|EMBL:KRS19724.1};
OS Roseovarius indicus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=540747 {ECO:0000313|EMBL:KRS19724.1, ECO:0000313|Proteomes:UP000051401};
RN [1] {ECO:0000313|EMBL:KRS19724.1, ECO:0000313|Proteomes:UP000051401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B108 {ECO:0000313|EMBL:KRS19724.1,
RC ECO:0000313|Proteomes:UP000051401};
RA Li G., Lai Q., Shao Z., Yan P.;
RT "The draft genome sequence of Roseovarius indicus B108T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QEW28923.1, ECO:0000313|Proteomes:UP000325785}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26383 {ECO:0000313|EMBL:QEW28923.1,
RC ECO:0000313|Proteomes:UP000325785};
RA Vollmers J., Petersen J.;
RT "Genetic Globetrotter - A new plasmid hitch-hiking vast phylogenetic and
RT geographic distances.";
RL Submitted (AUG-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 -!- 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; LAXI01000001; KRS19724.1; -; Genomic_DNA.
DR EMBL; CP031598; QEW28923.1; -; Genomic_DNA.
DR RefSeq; WP_057812915.1; NZ_LAXI01000001.1.
DR AlphaFoldDB; A0A0T5PFC7; -.
DR STRING; 540747.SAMN04488031_102738; -.
DR KEGG; rid:RIdsm_04764; -.
DR PATRIC; fig|540747.5.peg.510; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051401; Unassembled WGS sequence.
DR Proteomes; UP000325785; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UniProtKB-EC.
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; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000051401};
KW Transferase {ECO:0000313|EMBL:KRS19724.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 48..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..307
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 395..631
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..42
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 79149 MW; D98D7CE98981B1DF CRC64;
MSNNGRKKPR LVADDRRKKT TAKPKAKTTT ATKRKAAPKR RRKRSSNWVV RLFGGLFGWF
FRLVWAATWR ITAVVVLIIG MAVLYTYSTL PDVREVLDGR ARGSVTLRDR DGEVFAWRGD
QFGGVVTAET VSPHLKNAVV ATEDRRFYRH FGISPRGVAS AIRINLSEGR GPLSGHGGST
ITQQTAKLLC LGVQFDPDVW ESEQDYVQDC RRTTLWRKAK EAIYSLSMEA KYTKNEILSI
YLNRAYMGSG AFGAEAAAQR YFGKHAAEVT AQEAAMMAGL LTAPTRLAPT SNLERSQDRA
ATVLRLMREQ GYLSEAEMEE AQANPATLSE AAEAQTGGYF ADWVMESGPD FFTRDTTEDV
LIRTTLDQRI QRAAEEALKT VFEEKVKDGS KAQAAIVVMS ADGAVRAMVG GRKTKVTGAF
NRATMANRQT GSAFKPFVYA TALELGYSHN STVVDEPYCL SIPGSGRWCP ENYTRKHYGR
VTLTDALRRS LNVPAVKVSE AVGREKVRKV ASDFGIESSL ADGPALALGA SESTLLEMTG
AYAGILNGGS SVTPYGLVEL TLLGEDTPLM GTGGGIGERV IREEAAKELI FMMNQVVMSG
TGGRAKLPDR EVAGKTGTTQ AARDAWFLGF SADYVAGVWM GYDDNSPLQG VTGGGLPAEI
WRETMIRVHE GLEARPLPML RGQDVASDRD IDPRPEQPQQ QQPTQGRGES AVERILRDLL
GGGNR
//
