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Database: UniProt
Entry: A0A0C2Q7Y2_9CYAN
LinkDB: A0A0C2Q7Y2_9CYAN
Original site: A0A0C2Q7Y2_9CYAN 
ID   A0A0C2Q7Y2_9CYAN        Unreviewed;       411 AA.
AC   A0A0C2Q7Y2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=ATPase {ECO:0000313|EMBL:KIJ76303.1};
GN   ORFNames=SD81_17935 {ECO:0000313|EMBL:KIJ76303.1};
OS   Tolypothrix campylonemoides VB511288.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ76303.1};
RN   [1] {ECO:0000313|EMBL:KIJ76303.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB511288 {ECO:0000313|EMBL:KIJ76303.1};
RA   Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT   "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT   VB511288.";
RL   Submitted (JAN-2015) 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:KIJ76303.1}.
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DR   EMBL; JXCB01000008; KIJ76303.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2Q7Y2; -.
DR   OrthoDB; 9802602at2; -.
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   GO; GO:0006099; P:tricarboxylic acid cycle; 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   Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   PANTHER; PTHR11815:SF10; SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11815; SUCCINYL-COA SYNTHETASE BETA CHAIN; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   PIRSF; PIRSF001554; SucCS_beta; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 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|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          9..223
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   411 AA;  45282 MW;  262C9A8332D19C63 CRC64;
     MDLLEYQVKE WLAKKGIPVL PSQRIDHPTD LKRLKISYPI VLKSQVRAGE RAKAGGVRFV
     ETTIDAIAAA QNIFHLPILG ELPQVLLAEA KYDTEQEFYL AVVLDTAVCR PVLLGCTEAD
     DIDWESASEK MQHVVVQQEF SPFYARRLAL KMGLQGELIQ SVSTVVEKMY QLFVEKDLDL
     VEINPLGVSS SGQLMALNGN ISVNERAIGR HPDMAEMATK MVKTYISSDA VRNLGDWDVV
     EMHGKIAILG NGAGSVMATL DLVVNNGGKP GVCLNLRHAS VTETSPTTFR SRLEKALRNL
     STDKTIQVIL INLLGSISQA GEVSEVIANF VENNTSEVKP YMARSNGTKN RRESHFPRLV
     VRLAGSEFET ARKYIATLKT PTDGSIVVVE NLDEAVAEAA RLAKSTAYRR F
//
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