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Database: UniProt
Entry: C7PWH5_CATAD
LinkDB: C7PWH5_CATAD
Original site: C7PWH5_CATAD 
ID   C7PWH5_CATAD            Unreviewed;       418 AA.
AC   C7PWH5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   OrderedLocusNames=Caci_6401 {ECO:0000313|EMBL:ACU75255.1};
OS   Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL
OS   B-24433 / ID139908).
OC   Bacteria; Actinomycetota; Actinomycetes; Catenulisporales;
OC   Catenulisporaceae; Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU75255.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU75255.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647; DOI=10.4056/sigs.17259;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S., Chen F.,
RA   Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S., Mikhailova N.,
RA   Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Chain P.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Ali Z., Tindall B.J., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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DR   EMBL; CP001700; ACU75255.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7PWH5; -.
DR   STRING; 479433.Caci_6401; -.
DR   KEGG; cai:Caci_6401; -.
DR   eggNOG; COG3919; Bacteria.
DR   HOGENOM; CLU_041670_0_0_11; -.
DR   InParanoid; C7PWH5; -.
DR   OMA; DWFFHGY; -.
DR   Proteomes; UP000000851; 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; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   Pfam; PF02786; CPSase_L_D2; 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:UP000000851}.
FT   DOMAIN          138..340
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   418 AA;  45870 MW;  E10DA5080A9CEA0C CRC64;
     MVGMSLKASV DVDTATDAVL LKLDRNVFHH GGLGVIRSLG RLGIRVHAMR EDRFAPAGVS
     RYARRTVSPM PDRADPHDVL DLLDRLADRL PGPAVLITTD DAGAILLAEH GDKLRPRYLF
     PDPPADLPRR AAGKATLAEI CRAAGVPHPA TTVPVDAAEA TAFADACGYP VVAKVNLPWM
     ADRAAGLHST TVVRSREEML ALVQRARRAT GDGPDTGLLL QEYLAPAPCG TLQDWFFHGY
     FDADSRCLFG HTGIKVRSFP IHAGLTSYGR WESNERLRDE AVALLSGLGY RGPVDLDYRW
     DPRDDSYRLL DLNPRLGAQF RLFQDSAGID VVRAMHLDLT GRAFSPGEAV AGRSLFVENF
     DPIAALAYRR DENLTMRSWL ASVRAADEAA WFARDDLAPF FLTGARALWQ AAANRLRR
//
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