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Database: UniProt
Entry: A7GK89_BACCN
LinkDB: A7GK89_BACCN
Original site: A7GK89_BACCN 
ID   A7GK89_BACCN            Unreviewed;       411 AA.
AC   A7GK89;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   OrderedLocusNames=Bcer98_0177 {ECO:0000313|EMBL:ABS20547.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS20547.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS20547.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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DR   EMBL; CP000764; ABS20547.1; -; Genomic_DNA.
DR   RefSeq; WP_011983308.1; NC_009674.1.
DR   AlphaFoldDB; A7GK89; -.
DR   STRING; 315749.Bcer98_0177; -.
DR   GeneID; 56415708; -.
DR   KEGG; bcy:Bcer98_0177; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_029016_5_0_9; -.
DR   OrthoDB; 9803907at2; -.
DR   Proteomes; UP000002300; Chromosome.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR   PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR   Pfam; PF13535; ATP-grasp_4; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          105..307
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   411 AA;  47506 MW;  1463D6A7E4B9C6E3 CRC64;
     MNVLVIEPPL FMFEKFEKEA GRHDDKLYYV IKKTSKSKDE NILNLDIRDD FDVVVKYCEQ
     LNIDVIICIS EEYLLQASYL SECTGIFSVL TSDLVKNMRD KFLMKKIWTK ANILNASSIE
     YSESSIEEVQ SLNYPVIVKP NLGFSSSGVR LVHNLNELNS EILNIKMLNT LSTAISSEKI
     QPKILVEEFL CGDEYSADVI WQDGIPQFSK ILKKWIPQGN RFPDKLYHTI GEDEIDIETK
     ILQVVYQANR VLGMNNGATH TEVIVTKDDE IYVIETAARI GAGGIFSFIF EEKYGVEYLG
     LFYAIATNRR VDIKESMMLH EVDETLYYFS FDYPDYIDGT ICDIKGIDFL YEDKNIFERV
     FFKNKNDYIT TFASAEEYFL WILGKWPKNS SINALVERLV NLEKNIEIIV E
//
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