ID E6VMB3_RHOPX Unreviewed; 749 AA.
AC E6VMB3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN OrderedLocusNames=Rpdx1_0658 {ECO:0000313|EMBL:ADU42296.1};
OS Rhodopseudomonas palustris (strain DX-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=652103 {ECO:0000313|EMBL:ADU42296.1, ECO:0000313|Proteomes:UP000001402};
RN [1] {ECO:0000313|Proteomes:UP000001402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DX-1 {ECO:0000313|Proteomes:UP000001402};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Misra M., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Logan B., Oda Y., Harwood C.,
RA Woyke T.;
RT "Complete sequence of Rhodopseudomonas palustris DX-1.";
RL Submitted (DEC-2010) 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; CP002418; ADU42296.1; -; Genomic_DNA.
DR AlphaFoldDB; E6VMB3; -.
DR STRING; 652103.Rpdx1_0658; -.
DR KEGG; rpx:Rpdx1_0658; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_2_4_5; -.
DR OrthoDB; 9766909at2; -.
DR BioCyc; RPAL652103:RPDX1_RS03275-MONOMER; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001402; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 73..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 127..295
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 381..612
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 749 AA; 79336 MW; 00869438170CF42C CRC64;
MAWGRKTAGE RREPTFGPGE SLTDMRLTPQ DRVNLADDKP KKKSAGKPGG GARSKRKPRK
GMIASVRRAI GRVVYWSAVA GIWAVLAVVG VMVWVGAHLP PIQSLEIPKR PPTITIVADD
GSTMAVRGEQ AGTNVALKDL PPYLPKAFIA IEDRRFYSHF GVDPLGIGRA AVANVLHRGV
AQGGSTLTQQ LAKNLFLTQD RTLTRKLQEV ELALWLERKH SKAEILELYL NRVYFGSGAY
GVEAAAQKYF GKSAKEVTLV EAAMLAGLVK SPSRLAPNRN PEGAEKRAQI VLAAMAEAGF
VTAKQAQAAI ANPVYTVKPT GAGTINYVAD WIGEVLDDLV GQIDQSIIVE TSIDPRLQSV
AEAAIIDELA AKSVKYKVTQ GALVAMTPDG TVRAMIGGRN YADSQFNRAV TAKRQPGSAF
KPFVYLTAVE AGMTPETIRQ DAPLDLKGWK PENYSHEYFG AVTLTQALAM SLNTVAVRLG
LEVGPKNVVR TAHRLGIASK LDANPSIALG TSEVTLTELV GAYAAFANGG LLASPHVVKR
IRTAQGNKLL YARSNETASR VMDPRAAAMM NAMMQETLRS GTAQKADLPG WIAAGKTGTS
QDFRDAWFLG YTGTLVTGVW LGNDDNSPTR KATGGGLPVE VWTRFMREAL KGTTPQPLPG
GWSGGPLVTS GATGAASGSG IGGAIGGFLS GAAPTGGTIA QPGPRGEAQV TNMPPPPGAG
RMPPPTRANV RPEADAGLDG WLMDRLFGR
//
