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Database: UniProt
Entry: K2GWD4_9BACT
LinkDB: K2GWD4_9BACT
Original site: K2GWD4_9BACT 
ID   K2GWD4_9BACT            Unreviewed;       298 AA.
AC   K2GWD4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=ACD_3C00183G0003 {ECO:0000313|EMBL:EKE27630.1};
OS   uncultured bacterium (gcode 4).
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=1234023 {ECO:0000313|EMBL:EKE27630.1};
RN   [1] {ECO:0000313|EMBL:EKE27630.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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:EKE27630.1}.
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DR   EMBL; AMFJ01000457; EKE27630.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2GWD4; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF23; D-ALANINE--D-ALANINE LIGASE B; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          97..293
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   298 AA;  35582 MW;  07857390BAC5B1C6 CRC64;
     MKIALLTWWT WLEREVALMS ANTFNDNMDH EHDIFILPEE MGRFLGAYKD YDLALPVFHW
     EYWEDGTIFW LLDSIWLKYA FSPFAVHAIC MDKSKCNILV EKIWVKVPRS HLFRSKKEID
     SNKFSYPLIV KPNSWWSSVA TYKVNDFEEL EKAVENVISI TKDIVLVQEF ISGTEYSVPI
     IWNDALEALP IMRVELSAWE FFDYEEKYNS DWSNEVFWDI EEKLQNKLEN DSKKIHSFLG
     CRWISRIDFI VNESWVYFLE VNTIPGFSPA SIFPKAWKLT WRTLNQVVEK IIELWLEK
//
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