ID SUCC_STAA8 Reviewed; 388 AA.
AC Q2FZ37;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 13-FEB-2019, entry version 83.
DE RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558};
DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558};
DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558};
GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558};
GN OrderedLocusNames=SAOUHSC_01216;
OS Staphylococcus aureus (strain NCTC 8325).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W.,
RA Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press,
RL Washington D.C. (2006).
CC -!- FUNCTION: Succinyl-CoA synthetase functions in the citric acid
CC cycle (TCA), coupling the hydrolysis of succinyl-CoA to the
CC synthesis of either ATP or GTP and thus represents the only step
CC of substrate-level phosphorylation in the TCA. The beta subunit
CC provides nucleotide specificity of the enzyme and binds the
CC substrate succinate, while the binding sites for coenzyme A and
CC phosphate are found in the alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA;
CC Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00558};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00558};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC succinate from succinyl-CoA (ligase route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00558}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits.
CC {ECO:0000255|HAMAP-Rule:MF_00558}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}.
DR EMBL; CP000253; ABD30321.1; -; Genomic_DNA.
DR RefSeq; WP_001020801.1; NZ_LS483365.1.
DR RefSeq; YP_499753.1; NC_007795.1.
DR ProteinModelPortal; Q2FZ37; -.
DR SMR; Q2FZ37; -.
DR STRING; 93061.SAOUHSC_01216; -.
DR EnsemblBacteria; ABD30321; ABD30321; SAOUHSC_01216.
DR GeneID; 3919482; -.
DR KEGG; sao:SAOUHSC_01216; -.
DR PATRIC; fig|93061.5.peg.1115; -.
DR eggNOG; ENOG4105CMV; Bacteria.
DR eggNOG; COG0045; LUCA.
DR HOGENOM; HOG000007059; -.
DR KO; K01903; -.
DR OMA; VQIEINP; -.
DR BioCyc; GCF_000013425:G1I0R-1139-MONOMER; -.
DR BioCyc; SAUR93061:G1G5Y-1139-MONOMER; -.
DR UniPathway; UPA00223; UER00999.
DR PRO; PR:Q2FZ37; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR HAMAP; MF_00558; Succ_CoA_beta; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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 PANTHER; PTHR11815; PTHR11815; 1.
DR Pfam; PF08442; ATP-grasp_2; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF52210; SSF52210; 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; Metal-binding;
KW Nucleotide-binding; Reference proteome; Tricarboxylic acid cycle.
FT CHAIN 1 388 Succinate--CoA ligase [ADP-forming]
FT subunit beta.
FT /FTId=PRO_1000082244.
FT DOMAIN 9 244 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT NP_BIND 53 55 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT REGION 321 323 Substrate binding; shared with subunit
FT alpha. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT METAL 199 199 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT METAL 213 213 Magnesium. {ECO:0000255|HAMAP-
FT Rule:MF_00558}.
FT BINDING 46 46 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 99 99 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 102 102 ATP; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 107 107 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}.
FT BINDING 264 264 Substrate; shared with subunit alpha.
FT {ECO:0000255|HAMAP-Rule:MF_00558}.
SQ SEQUENCE 388 AA; 42056 MW; 475D6D47FE489DC9 CRC64;
MNIHEYQGKE IFRSMGVAVP EGRVAFTAEE AVEKAKELNS DVYVVKAQIH AGGRGKAGGV
KIAKSLSEVE TYAKELLGKT LVTHQTGPEG KEIKRLYIEE GCAIQKEYYV GFVIDRATDQ
VTLMASEEGG TEIEEVAAKT PEKIFKETID PVIGLSPFQA RRIAFNINIP KESVNKAAKF
LLALYNVFIE KDCSIVEINP LVTTADGDVL ALDAKINFDD NALFRHKDVV ELRDLEEEDP
KEIEASKHDL SYIALDGDIG CMVNGAGLAM ATMDTINHFG GNPANFLDAG GSATREKVTE
AFKIILGDEN VKGIFVNIFG GIMKCDVIAE GIVEAVKEVD LTLPLVVRLE GTNVELGKKI
LKDSGLAIEP AATMAEGAQK IVKLVKEA
//
