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Database: UniProt
Entry: A0A2C1YYB6_9BACI
LinkDB: A0A2C1YYB6_9BACI
Original site: A0A2C1YYB6_9BACI 
ID   A0A2C1YYB6_9BACI        Unreviewed;       341 AA.
AC   A0A2C1YYB6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=COD92_20040 {ECO:0000313|EMBL:PGV49875.1};
OS   Bacillus sp. AFS037270.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV49875.1, ECO:0000313|Proteomes:UP000225442};
RN   [1] {ECO:0000313|EMBL:PGV49875.1, ECO:0000313|Proteomes:UP000225442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS037270 {ECO:0000313|EMBL:PGV49875.1,
RC   ECO:0000313|Proteomes:UP000225442};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:PGV49875.1}.
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DR   EMBL; NUNF01000041; PGV49875.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C1YYB6; -.
DR   Proteomes; UP000225442; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; IPR048764; PylC_PurT_N.
DR   PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF15632; ATPgrasp_Ter; 1.
DR   Pfam; PF21360; PylC-like_N; 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   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          122..299
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   341 AA;  38849 MW;  F1C7E9B4C579C523 CRC64;
     MNKLNILITG SGSIYGSAVI QSLLNSKLNV HLVATDTHSL AIGLHIAHRS YLVPPVKEEQ
     HYLEKVLEIL TKEKIHALFI ASAQELPFYS QYKALIEHQT GAKVFTNTTK VLSICNDKWN
     TVNFLKEHNF HFPITIRYPE DKEQISSFIQ EVGFPFIAKP RHGKGSEDIH VVKDLSYLKL
     VLLEKKDMIF QQYLPNDQEE YTVGICCGEN GKVLSSIALK RYLQDGITMV AKSDDFNSIT
     NYCQEIAKAL KPYGPCNFQL RLWNGSPYIF EINPRFSSTT GMRALLGVNE PEILLQAELL
     GKDIQEINIL KSTVIRQYSD TLVPTEQIEK LEQERFIDNK E
//
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