ID SUCC_CAMJJ Reviewed; 387 AA.
AC A1VYP2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 01-MAY-2013, entry version 52.
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=CJJ81176_0558;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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 succinate from succinyl-CoA (ligase route): step 1/1.
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; CP000538; EAQ73087.1; -; Genomic_DNA.
DR RefSeq; YP_001000233.1; NC_008787.1.
DR ProteinModelPortal; A1VYP2; -.
DR STRING; 354242.CJJ81176_0558; -.
DR PRIDE; A1VYP2; -.
DR EnsemblBacteria; EAQ73087; EAQ73087; CJJ81176_0558.
DR GeneID; 4682667; -.
DR KEGG; cjj:CJJ81176_0558; -.
DR PATRIC; 20051069; VBICamJej103413_0566.
DR eggNOG; COG0045; -.
DR HOGENOM; HOG000007059; -.
DR KO; K01903; -.
DR OMA; QPVTKIL; -.
DR ProtClustDB; PRK00696; -.
DR UniPathway; UPA00223; UER00999.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:HAMAP.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR Gene3D; 3.30.1490.20; -; 1.
DR Gene3D; 3.30.470.20; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
DR HAMAP; MF_00558; Succ_CoA_beta; 1; -.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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 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; CoA_ligase; 1.
DR TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR PROSITE; PS50975; ATP_GRASP; FALSE_NEG.
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 1 387 Succinyl-CoA ligase [ADP-forming] subunit
FT beta.
FT /FTId=PRO_1000082055.
FT DOMAIN 9 244 ATP-grasp.
FT NP_BIND 35 108 ATP (By similarity).
FT METAL 197 197 Magnesium or manganese (By similarity).
FT METAL 199 199 Magnesium or manganese (By similarity).
SQ SEQUENCE 387 AA; 41742 MW; 8A85A94A7A2B27A5 CRC64;
MNIHEYQAKA IFADNSIPTL KGKVAFSVDE AVANAKELGG SVWAVKAQIH AGGRGLGGGV
KIAKNLDEVK DYASKILGMN LVTHQTGPEG KLVQKLYIES GANIVKEYYL AILFNRMAEQ
ITIIASSEGG MDIEKVAKES PEKIAKVGID PQIGFKMFHG LEVAKVLGLD KDESKKLISM
IAKLYKLYMD KDMNMLEINP LIKTAEGDFY ALDAKCSFDD SALYRHPEIA ELRDITEENP
AEREAAEFGL SYVKLDGDVA CMVNGAGLAM ATMDIINYSG AKPANFLDVG GGASAETVAK
AFEIILRDKN VKVIFINIFG GIVRCDRIAN GILEATKNVE VNIPIVVRLD GTNAAEAKTI
LDNSNLKNIK AATNLKNGAE LVKSLVG
//
