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Database: UniProt
Entry: Q6TTJ7_9BACI
LinkDB: Q6TTJ7_9BACI
Original site: Q6TTJ7_9BACI 
ID   Q6TTJ7_9BACI            Unreviewed;       167 AA.
AC   Q6TTJ7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Succinyl-CoA synthetase beta subunit {ECO:0000313|EMBL:AAQ90513.1};
DE   Flags: Fragment;
GN   Name=sucC {ECO:0000313|EMBL:AAQ90513.1};
OS   Bacillus sp. AH 1132.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=247838 {ECO:0000313|EMBL:AAQ90513.1};
RN   [1] {ECO:0000313|EMBL:AAQ90513.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AH 1132 {ECO:0000313|EMBL:AAQ90513.1};
RX   PubMed=14711642; DOI=10.1128/AEM.70.1.191-201.2004;
RA   Helgason E., Tourasse N.J., Meisal R., Caugant D.A., Kolsto A.B.;
RT   "Multilocus sequence typing scheme for bacteria of the Bacillus cereus
RT   group.";
RL   Appl. Environ. Microbiol. 70:191-201(2004).
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DR   EMBL; AY387894; AAQ90513.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6TTJ7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR005811; SUCC_ACL_C.
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   Pfam; PF00549; Ligase_CoA; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          2..58
FT                   /note="ATP-grasp fold succinyl-CoA synthetase-type"
FT                   /evidence="ECO:0000259|Pfam:PF08442"
FT   DOMAIN          118..167
FT                   /note="ATP-citrate synthase/succinyl-CoA ligase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00549"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAQ90513.1"
FT   NON_TER         167
FT                   /evidence="ECO:0000313|EMBL:AAQ90513.1"
SQ   SEQUENCE   167 AA;  18433 MW;  6FD078E6EC5D378D CRC64;
     FKEYIDPAVG LQGFQARRIA FNINIPKELV GQAVKFMMGL YRAFIEKDCS IAEINPLVTT
     GEGKVMALDA KLNFDSNALY RHKDILELRD LDEEDSKEIE ASKYDLNYIP LDGNIGCMVN
     GAGLAMATMD IIKHYHGDPA NFLDVGGGAT AEKVTEAFKI ILSDKNV
//
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