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Database: UniProt
Entry: K0UIS9_MYCVA
LinkDB: K0UIS9_MYCVA
Original site: K0UIS9_MYCVA 
ID   K0UIS9_MYCVA            Unreviewed;       790 AA.
AC   K0UIS9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
DE   Flags: Fragment;
GN   ORFNames=MVAC_20628 {ECO:0000313|EMBL:EJZ06771.1};
OS   Mycolicibacterium vaccae ATCC 25954.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1194972 {ECO:0000313|EMBL:EJZ06771.1, ECO:0000313|Proteomes:UP000006072};
RN   [1] {ECO:0000313|EMBL:EJZ06771.1, ECO:0000313|Proteomes:UP000006072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25954 {ECO:0000313|EMBL:EJZ06771.1,
RC   ECO:0000313|Proteomes:UP000006072};
RX   PubMed=23105074; DOI=10.1128/JB.01462-12;
RA   Ho Y.S., Adroub S.A., Abadi M., Al Alwan B., Alkhateeb R., Gao G.,
RA   Ragab A., Ali S., van Soolingen D., Bitter W., Pain A., Abdallah A.M.;
RT   "Complete Genome Sequence of Mycobacterium vaccae Type Strain ATCC 25954.";
RL   J. Bacteriol. 194:6339-6340(2012).
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:EJZ06771.1}.
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DR   EMBL; ALQA01000052; EJZ06771.1; -; Genomic_DNA.
DR   AlphaFoldDB; K0UIS9; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_6_1_11; -.
DR   Proteomes; UP000006072; 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   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF34; PENICILLIN-BINDING PROTEIN 1A; 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   Transferase {ECO:0000313|EMBL:EJZ06771.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        78..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          122..300
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          394..659
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          742..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..49
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         790
FT                   /evidence="ECO:0000313|EMBL:EJZ06771.1"
SQ   SEQUENCE   790 AA;  82565 MW;  FEC5B2E48CEF885D CRC64;
     MRDGVPPPLR DPVDAVKRAL DGRPAKQPPK QPPKQPPKQP PPPRGGPPSA YGPGGGGPTG
     PRRSLREQIN WTWVRRGAIV AAALLIVLPL LTFGMAYMIV DVPKPGDIRT AQVSTILASD
     GSEIAKIVPP EGNRVDVNID QIPVHVRDAV MAAEDRDFYS NPGFSFTGFL RAAKNNIFGG
     DLQGGSTITQ QYVKNALVGD ARSGVGGVIR KAKELVISTK MSSEWSKDQV LQSYLNIIYF
     GRGAYGVAAA AQSYFGKPVE QVTVSEGALL AALIQRPSVL DPAVDPDASA IRWSWVLDGM
     VEIGALSPEE RQAQVFPATI PPDQAFTQNQ TTGPNGLIER QVVNELMEIF DINEQTLNTE
     GLQITTTIDP KAQEAAVDAV EEYLDGQDPD MRTAVVSIDP KTGGVKAYYG GSDANGFDFA
     QAGLPTGSSF KVFALVAALQ QGMGLGYQVD SSPVEVNGIK ISNVEGNSCG TCNIAEALKR
     SLNTSYYRLM LQLKNGPQDV ADAAHTAGIA ESIPGIEHTL SEDGQGGPPN NGVVLGQYQS
     RVIDMASAYA TLAASGVYHK PHFVQKVVNA EGTVLFDAGQ EDNAGEQRID KAVADNVTAA
     MQPIAAYSNG HALAGGRPSA AKTGTNQLGD TGANRDAWMV GFTPSLSTAV WVGTVDGNKP
     LENKWGSPVY GSGLPSDIWK ATMDGALDGT DNESFPKPEE IGGYAGVPQA PPPPRTTEAP
     IPSETVIQPT LEIAPGITIP WGPPTTVPVT PPGAPVPDAG VPGAPVPPGA PGQPGAPLPP
     GAPVPPGAPP
//
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