ID A0A1F6DYB7_9BACT Unreviewed; 340 AA.
AC A0A1F6DYB7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN ORFNames=A3D71_04770 {ECO:0000313|EMBL:OGG66337.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPHIGHO2_02_FULL_55_20.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798497 {ECO:0000313|EMBL:OGG66337.1, ECO:0000313|Proteomes:UP000177652};
RN [1] {ECO:0000313|EMBL:OGG66337.1, ECO:0000313|Proteomes:UP000177652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG66337.1}.
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DR EMBL; MFLK01000012; OGG66337.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6DYB7; -.
DR STRING; 1798497.A3D71_04770; -.
DR Proteomes; UP000177652; Unassembled WGS sequence.
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 Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR011095; Dala_Dala_lig_C.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF07478; Dala_Dala_lig_C; 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}.
FT DOMAIN 75..335
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 340 AA; 38472 MW; E1687FE06902BCFC CRC64;
MYAPRMRKKS EHLVLAGMLQ KLGKKIGARV VLEPEWKIAG QIRFGNGRNS YFRYNTLDLN
PVGASDIAKD KDYANFFMRK MGYPTIRGKS FFSDEWCKII GSRRNTDAGY RYATKLGLPV
IVKPNSGTQG IDVALVHTKK DFYRAMKQIF KHDRIALVQK QVHGRDYRIV VLDKEIISAY
ERIPLNVVGD GHSTIKQLLA RKARAFLASS RDTAINLKDP RIAAKLKHQG RSLTYVPRRG
EQVFLLDNAN LSSGGDAVDV TNNIHPAFKK LAIKLTKDMG LRLCGVDLMV YGDIREKPKK
YWVLEINAAP GLDHYVKTGK AQQKIVENLY LKVLKSLARP
//
