UniProt: A0A0G3AJ26

Database: UniProt
Entry: A0A0G3AJ26_9ACTN

LinkDB:  A0A0G3AJ26_9ACTN 
Original site:  A0A0G3AJ26_9ACTN

All links

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)   
Literature (1)   
   PubMed (1)   
All databases (16)   

Download RDF

ID   A0A0G3AJ26_9ACTN        Unreviewed;       773 AA.
AC   A0A0G3AJ26;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, 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   ORFNames=ABB07_17460 {ECO:0000313|EMBL:AKJ11760.1};
OS   Streptomyces incarnatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=665007 {ECO:0000313|EMBL:AKJ11760.1, ECO:0000313|Proteomes:UP000035366};
RN   [1] {ECO:0000313|EMBL:AKJ11760.1, ECO:0000313|Proteomes:UP000035366}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL8089 {ECO:0000313|Proteomes:UP000035366};
RX   PubMed=26159526;
RA   Oshima K., Hattori M., Shimizu H., Fukuda K., Nemoto M., Inagaki K.,
RA   Tamura T.;
RT   "Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces
RT   the Nucleoside Antibiotic Sinefungin.";
RL   Genome Announc. 3:e00715-e00715(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   ---------------------------------------------------------------------------
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; CP011497; AKJ11760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G3AJ26; -.
DR   STRING; 665007.ABB07_17460; -.
DR   PATRIC; fig|665007.5.peg.3738; -.
DR   Proteomes; UP000035366; 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; 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   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   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        20..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..261
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          362..635
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          451..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          688..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  81624 MW;  0068259EBEA3BAB3 CRC64;
     MPKKRSGGGL SPTQQAAKFL GVSVLAGAVM AGIALPAAGA LGLAAKGSVQ SFDEIPANLK
     SPQLSQRTTI LDNQGNQIAA VYSRDRTVVD LKDISPYMQK AIVAIEDSRF YQHGAIDLKG
     VLRALNKNAQ EGGVAQGAST LTQQLVKNYF IEEAGDDPTK VAEATQQTLG RKIKELKYAI
     QIEEKLGKKK ILENYLNITF FGEQAYGVEA ASQRYFSKHA KDLNLQESAL LAGIVQSPSR
     YDPVNDEAEA TKRRNTVLQR MAEVGDISQQ EADEAKAKPL GLHPSQPKNG CITAVKGAGF
     FCDYVRDVVL NDPVFGRTKE ARAKLWNQGG LTIRTTLDPQ AQDSVQASIK QHVYQSDAVA
     TAATIVEPGT GKILAMGQSR PYGFGQNETQ INLSVNSDMG GGAGYQPGST FKPIVAAAAI
     EGGKPPTQQY SSPYEMPYPD QVQACDGKVW RNDPNKPAKL TNENESEHGP MGMKEATAKS
     VNTYYVQLIS DIGICPVTEM AKKMGVHRAD GRAIDQAPSI ALGTQEVSPL TMANAYATFA
     SRGMYCTPVA IESITQKVGS VQKSLQVPKS TCSRAMSEKT ADTVSTLLKG VVEDGTGREA
     GLGDRPSAGK TGTTDERYAA WFVGYTPNMA GAVWVGDPAH KRQMKNISIG GVWNDKVYGG
     QVPGPIWRDM MTGALSGKPV EDFHLIDIPD DNKKGDGQGK GHGGNDGGKN GDSTGGIGGL
     IGGLTAGGTA DGGTTGATTG GPFPTPTFSL PGNFIQGQTN GGNKGNGNGG WRG
//

DBGET integrated database retrieval system