ID A0A0E3U3D1_9ENTR Unreviewed; 390 AA.
AC A0A0E3U3D1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta {ECO:0000313|EMBL:AKC59902.1};
GN Name=sucC {ECO:0000313|EMBL:AKC59902.1};
GN ORFNames=BTURN675_326 {ECO:0000313|EMBL:AKC59902.1};
OS Blochmannia endosymbiont of Polyrhachis (Hedomyrma) turneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=1505596 {ECO:0000313|EMBL:AKC59902.1, ECO:0000313|Proteomes:UP000033094};
RN [1] {ECO:0000313|EMBL:AKC59902.1, ECO:0000313|Proteomes:UP000033094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=675 {ECO:0000313|EMBL:AKC59902.1,
RC ECO:0000313|Proteomes:UP000033094};
RX PubMed=25861561;
RA Williams L.E., Wernegreen J.J.;
RT "Genome evolution in an ancient bacteria-ant symbiosis: parallel gene loss
RT among Blochmannia spanning the origin of the ant tribe Camponotini.";
RL PeerJ 3:E881-E881(2015).
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DR EMBL; CP010048; AKC59902.1; -; Genomic_DNA.
DR RefSeq; WP_046288812.1; NZ_CP010048.1.
DR AlphaFoldDB; A0A0E3U3D1; -.
DR STRING; 1505596.BTURN675_326; -.
DR KEGG; bed:BTURN675_326; -.
DR PATRIC; fig|1505596.4.peg.332; -.
DR HOGENOM; CLU_037430_0_2_6; -.
DR OrthoDB; 9802602at2; -.
DR Proteomes; UP000033094; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
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; IPR011761; ATP-grasp.
DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR005809; Succ_CoA_ligase-like_bsu.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01016; sucCoAbeta; 1.
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 PIRSF; PIRSF001554; SucCS_beta; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AKC59902.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000033094};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 9..228
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 390 AA; 43347 MW; 1FC0255458FDB5F1 CRC64;
MNLYEYQAKQ LLAKYNLPIP NGNVCSTLNQ AKEYIKHTKG PWVGKCQIQA GGRGKSGGVE
VLKSENEVQY FITHWLGKRL ITDQTDDDGE IVHNILLEPY FCVINELYLS MSIDRTNEGI
VCLVSSKGGV EIEKIAQETP HVIKKIFLDP LMGPQIYQAR KLGFSLRLNM DQIKQFTNIF
MNIGKMFLTY DLMLIEINPL VIIDNNHLLC LDAKIHIDHN ALFRQKKMLL TDNIIQNISN
TSLLCSDNTN LKFNYVPMKG NIGCIVNGAG LAMATMDLLS LYGGNVANFL DVGGDVTKES
VIESVKTIIY NHKVKVILIN IFGGIVCCNL IAEGIIKALS TLNIMIPIVV RLQGNNAISG
NKQLANSKHH IIASDNLFNA IQTVISIANK
//
