UniProt: A0A0D3LG01

Database: UniProt
Entry: A0A0D3LG01_9BACT

LinkDB:  A0A0D3LG01_9BACT 
Original site:  A0A0D3LG01_9BACT

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (5)   
   Pfam (2)   
All databases (15)   

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ID   A0A0D3LG01_9BACT        Unreviewed;       791 AA.
AC   A0A0D3LG01;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=D770_13935 {ECO:0000313|EMBL:AHM61041.1};
OS   Flammeovirgaceae bacterium 311.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX   NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM61041.1, ECO:0000313|Proteomes:UP000064112};
RN   [1] {ECO:0000313|EMBL:AHM61041.1, ECO:0000313|Proteomes:UP000064112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=311 {ECO:0000313|EMBL:AHM61041.1,
RC   ECO:0000313|Proteomes:UP000064112};
RA   Fang C.;
RT   "Complete bacteria genome obtained just from illumina data.";
RL   Submitted (NOV-2012) 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}.
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DR   EMBL; CP004371; AHM61041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D3LG01; -.
DR   STRING; 1257021.D770_13935; -.
DR   KEGG; fbt:D770_13935; -.
DR   PATRIC; fig|1257021.3.peg.3160; -.
DR   Proteomes; UP000064112; 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: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; 2.
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   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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   ECO:0000313|EMBL:AHM61041.1}; 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:UP000064112};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        23..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          84..277
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          451..693
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          766..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..783
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   791 AA;  88468 MW;  F17031EC8078AF10 CRC64;
     MATTETPVKK KKKKTKSGTK QKVLGGIVIA LWVLFFGVVI GLPLYIYSVS TNFLGLYGGM
     PGFSTLENPE NDLSSELYSS DGVQLGKYYR KNRVNATYEE LSPNLVKALI AIEDVRFEGH
     SGIDPESMGR VAFGVVKYAF TGNKDNLEGG GSTLSQQLAK NLFSLRSDER YEGKLYGINR
     NIDMLFNKTK EWITAVRLER SYTKKEILAM YLNTVEFGSN SYGIKTASQT FYGKNPNELD
     VQEAATLAGI VQAPSRLSPF YHPEAAQLKR NTVVLKMAEH DYISKSTADS ILQQPLALKY
     SVESHNQGVA PYFRSVIKDF LTKWAREHGY DIYEDGLKIY TTIDSRLQKY AEEAVAGHMG
     KLQTKFEKEW AGRNPWVDEN NREISGFIEQ EAKRSEHYQK LVRKYGKGAD SVDIVMKAKR
     PMRIFSYKGE IDTLMSPLDS VRHYKRFLHT GFMAMDPYSG AIRAWVGGID FKHFKFDHVM
     QSKRQPGSTF KPFVYATAIE NGYSPCYTIY DVPRSYPTGG DPPSWEPKNS DGKFTNQPMS
     LREAMAQSIN SVTADIMYKM KPENVVSLAR RMGIKSDLEP VLALALGTSD VSVYEMVGAY
     STFVNKGVYT QPFFITRIED KNGNVLFEPQ PKTIEALNEE TAYLMVHMLK GGTQLGGGTA
     LGLSPQLRHN IEIGAKTGTT QNASDGWFMG ITPELVAGAW VGGDNRSIRF RSWLSGQGAR
     TAMPIWEDFM LKAYNDPQLD IDKTTFDAPR EPLSIEINCA RYNQNYGGAS TNEPDTSGIN
     TQAPIDPGDI F
//

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