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Database: UniProt
Entry: B8GMV1_THISH
LinkDB: B8GMV1_THISH
Original site: B8GMV1_THISH 
ID   B8GMV1_THISH            Unreviewed;       263 AA.
AC   B8GMV1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=RimK domain protein ATP-grasp {ECO:0000313|EMBL:ACL73766.1};
GN   OrderedLocusNames=Tgr7_2691 {ECO:0000313|EMBL:ACL73766.1};
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL73766.1, ECO:0000313|Proteomes:UP000002383};
RN   [1] {ECO:0000313|EMBL:ACL73766.1, ECO:0000313|Proteomes:UP000002383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL73766.1,
RC   ECO:0000313|Proteomes:UP000002383};
RX   PubMed=21475584;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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DR   EMBL; CP001339; ACL73766.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8GMV1; -.
DR   STRING; 396588.Tgr7_2691; -.
DR   KEGG; tgr:Tgr7_2691; -.
DR   eggNOG; COG0189; Bacteria.
DR   HOGENOM; CLU_075266_0_0_6; -.
DR   OMA; DHAGFDI; -.
DR   OrthoDB; 1704979at2; -.
DR   Proteomes; UP000002383; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF08443; RimK; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002383}.
FT   DOMAIN          75..263
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   263 AA;  29507 MW;  49201991C10E5FCD CRC64;
     MRLLSFDAYR SFGIPDTRYL KPELMYRHEA EILAADWLLF PASWQVDVLA WVYNKRLFPS
     IQSYHLGHDK VRMTRALWAA APAHVPETLI LPSTPAALEE ILDTFSFPLV LKEPRSAEGR
     GVALIEDRQA LRDWAATHDV LYAQERLPIE RDVRVTVVGD QVVAAYWRKA PQGGFHNNIA
     RGGELIFEDV PPQAVSLVAD LARRLKIDHA GFDVALVDGH PFILEFNVLF GNGGLEPLGV
     KLADVIHQYL SRETPGPTLQ VVS
//
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