ID   SUCC_BAUCH              Reviewed;         393 AA.
AC   Q1LTZ4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta;
DE            EC=6.2.1.5;
DE   AltName: Full=Succinyl-CoA synthetase subunit beta;
DE            Short=SCS-beta;
GN   Name=sucC; OrderedLocusNames=BCI_0097;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR   EMBL; CP000238; ABF14132.1; -; Genomic_DNA.
DR   RefSeq; YP_588570.1; -.
DR   GeneID; 4056318; -.
DR   GenomeReviews; CP000238_GR; BCI_0097.
DR   KEGG; bci:BCI_0097; -.
DR   HOGENOM; Q1LTZ4; -.
DR   OMA; Q1LTZ4; NLHCLDA.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:HAMAP.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR   HAMAP; MF_00558; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1.
DR   PANTHER; PTHR11815; CoA_lig_beta; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Tricarboxylic acid cycle.
FT   CHAIN         1    393       Succinyl-CoA ligase [ADP-forming] subunit
FT                                beta.
FT                                /FTId=PRO_1000082022.
FT   DOMAIN        9    245       ATP-grasp.
FT   NP_BIND      35    108       ATP (By similarity).
FT   METAL       198    198       Magnesium or manganese (By similarity).
FT   METAL       200    200       Magnesium or manganese (By similarity).
SQ   SEQUENCE   393 AA;  43179 MW;  DC2255021012D409 CRC64;
     MKLHEYQAKM LFAQYGIPIP KGLVCTTPNE AKESIAVIGY GPWIVKCQVH AGGRGKSGGV
     RIVRSKEEIQ EFAKQWFGKH LITEQTNHIG QPVSKILVEA AIDIAQELYL GCLVDRSNQC
     IKFIASIQGG IDIENIAKEK PHLLHQIILD PLIGPQLYQS RDLAFKIGLS SKKQINQFNK
     IFMGLATLFL EKDLVMAEIN PLVITRLGDL ICLDGKLHVD SNALFRQPEL CKMLDPSQED
     KCETYAKQHN LNYIALNGNI GCLVNGAGLA MSTIDMVKFY GGEPANFLDV GGRVTQEKVT
     KAFQIILSDK KVKVILVNIF GGIVCCDVIA KGIINARLES GINIPVIVRL EGNNAKQGIQ
     HLVNSILNIR IATNLTTAAK QAVALVEGKQ CLF
//