ID A0A0L0LAG5_9BACT Unreviewed; 733 AA.
AC A0A0L0LAG5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=mrcA {ECO:0000313|EMBL:KND46875.1};
GN ORFNames=AB199_00385 {ECO:0000313|EMBL:KND46875.1};
OS Parcubacteria bacterium C7867-004.
OC Bacteria; Candidatus Parcubacteria.
OX NCBI_TaxID=1659198 {ECO:0000313|EMBL:KND46875.1, ECO:0000313|Proteomes:UP000036787};
RN [1] {ECO:0000313|EMBL:KND46875.1, ECO:0000313|Proteomes:UP000036787}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7867-004 {ECO:0000313|EMBL:KND46875.1};
RX PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA Nelson W.C., Stegen J.C.;
RT "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT symbiotic lifestyle.";
RL Front. Microbiol. 6:713-713(2015).
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:KND46875.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFCN01000006; KND46875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0LAG5; -.
DR STRING; 1659198.AB199_00385; -.
DR PATRIC; fig|1659198.3.peg.67; -.
DR Proteomes; UP000036787; 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:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:KND46875.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KND46875.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transferase {ECO:0000313|EMBL:KND46875.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..248
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 337..601
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 712..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 79931 MW; 4AB13B110862542E CRC64;
MSKGIKKRGG LHKHLADPHP LLRVAYFLVG ALLLVAGAGI LWAALTPIPD LNSFDSRKVA
QSTKIYDRTG KTVLYDLNHD VRRNVVTLSE ISPNLQKAAI AIEDSDFYHH SGVSFTSTAR
AIIVDIKTQS FAQGGSTITQ QVVKNTILSG RKDLIRKFQE WVLAWKLEQR YTKNQILEFY
FNVTPYGGTL YGAEVASRAF FGKSASDLSV AEAAYLAAIP QLPTYYSPYG NNRKDLDERK
DLVLSRMKVL GYLTEEEYQA AKKDEVIFSR QRDNSILAPH FVFYIEQQLE QKYGPDVVTE
GLSVITTLDA ELQNAAQTIV KDYATANTAK FNASNAALVA IDPKTGQILA MVGSRDYFDE
DIDGNYNSAI ALRQPGSSFK PFVYATALEK GYTPESVVFD LPTQFSTVCA ASETTNSEPP
CYAPGNYDDK FRGPMTFTTA LAQSINIPAV QTLYLAGIKN VIGLAERLGI TTLGDAKEYG
LSFALGAAEV KLLDLVSAYS VFANDGVRNP AVGILEIRDM KGKVIEKFTA APQQAIDAGV
ARQISSMLSN NEARFPEYPP NNPLHFNEYD VAAKTGTTNE SRDAWTVGFT PTIAVGVWAG
NNNNTPMVKE IAGYIVAPMW HAFMAEALQK MPEEVFNEPP AISESAAPAL RGIIYVPSGA
GTQAHSLLHW TDKENPLGPP PANPFRDPQY AYWEYPIQTW LANGSPTLFG AQATSTASST
PGIGIDGSDI GGQ
//
