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Database: UniProt/TrEMBL
Entry: Q2YXM0_STAAB
LinkDB: Q2YXM0_STAAB
Original site: Q2YXM0_STAAB 
ID   Q2YXM0_STAAB            Unreviewed;       302 AA.
AC   Q2YXM0;
DT   20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2005, sequence version 1.
DT   29-OCT-2014, entry version 66.
DE   RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit alpha {ECO:0000256|RuleBase:RU000699};
DE            EC=6.2.1.5 {ECO:0000256|RuleBase:RU000699};
GN   OrderedLocusNames=SAB1110 {ECO:0000313|EMBL:CAI80799.1};
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=273036 {ECO:0000313|EMBL:CAI80799.1, ECO:0000313|Proteomes:UP000001927};
RN   [1] {ECO:0000313|EMBL:CAI80799.1, ECO:0000313|Proteomes:UP000001927}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1 {ECO:0000313|Proteomes:UP000001927};
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA. {ECO:0000256|RuleBase:RU000699}.
CC   -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC       {ECO:0000256|RuleBase:RU000699}.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha
CC       subunit family. {ECO:0000256|RuleBase:RU000677}.
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DR   EMBL; AJ938182; CAI80799.1; -; Genomic_DNA.
DR   RefSeq; YP_416590.1; NC_007622.1.
DR   ProteinModelPortal; Q2YXM0; -.
DR   SMR; Q2YXM0; 2-284.
DR   STRING; 273036.SAB1110; -.
DR   EnsemblBacteria; CAI80799; CAI80799; SAB1110.
DR   GeneID; 3795071; -.
DR   KEGG; sab:SAB1110; -.
DR   PATRIC; 19523067; VBIStaAur92441_1182.
DR   eggNOG; COG0074; -.
DR   HOGENOM; HOG000239685; -.
DR   KO; K01902; -.
DR   OMA; HIPVHDE; -.
DR   OrthoDB; EOG644ZT0; -.
DR   BioCyc; SAUR273036:GJVS-1132-MONOMER; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003878; F:ATP citrate synthase activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.261; -; 1.
DR   Gene3D; 3.40.50.720; -; 1.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF52210; SSF52210; 1.
DR   TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000699};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001927};
KW   Ligase {ECO:0000256|RuleBase:RU000677, ECO:0000313|EMBL:CAI80799.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000699}.
FT   ACT_SITE    247    247       Tele-phosphohistidine intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR001553-1}.
SQ   SEQUENCE   302 AA;  31542 MW;  C05AFD1B8DCC69E4 CRC64;
     MSVFIDKNTK VMVQGITGST ALFHTKQMLD YGTKIVAGVT PGKGGQVVEG VPVFNTVEEA
     KNETGATVSV IYVPAPFAAD SILEAADADL DMVICITEHI PVLDMVKVKR YLQGRKTRLV
     GPNCPGVITA DECKIGIMPG YIHKKGHVGV VSRSGTLTYE AVHQLTEEGI GQTTAVGIGG
     DPVNGTNFID VLKAFNEDDE TKAVVMIGEI GGTAEEEAAE WIKANMTKPV VGFIGGQTAP
     PGKRMGHAGA IISGGKGTAE EKIKTLNSCG VKTAATPSEI GSTLIEAAKE AGIYESLLTV
     NK
//
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