DHSC_SALTI
ID DHSC_SALTI Reviewed; 129 AA.
AC P63726; Q8XG40;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Succinate dehydrogenase cytochrome b556 subunit;
DE Short=Cytochrome b-556;
GN Name=sdhC; OrderedLocusNames=STY0775, t2144;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000250};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC flavoprotein, an iron-sulfur protein, plus two membrane-anchoring
CC proteins, SdhC and SdhD. The complex can form homotrimers (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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DR EMBL; AL513382; CAD05194.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69758.1; -; Genomic_DNA.
DR RefSeq; NP_455288.1; NC_003198.1.
DR RefSeq; WP_001539490.1; NZ_FFOJ01000008.1.
DR AlphaFoldDB; P63726; -.
DR SMR; P63726; -.
DR STRING; 220341.16501964; -.
DR EnsemblBacteria; AAO69758; AAO69758; t2144.
DR KEGG; stt:t2144; -.
DR KEGG; sty:STY0775; -.
DR PATRIC; fig|220341.7.peg.780; -.
DR eggNOG; COG2009; Bacteria.
DR HOGENOM; CLU_094691_2_1_6; -.
DR OMA; YHLVAGI; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045281; C:succinate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR018495; Succ_DH_cyt_bsu_CS.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR PANTHER; PTHR10978; PTHR10978; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000178; SDH_cyt_b560; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1.
DR PROSITE; PS01000; SDH_CYT_1; 1.
DR PROSITE; PS01001; SDH_CYT_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Transmembrane; Transmembrane helix; Transport;
KW Tricarboxylic acid cycle.
FT CHAIN 1..129
FT /note="Succinate dehydrogenase cytochrome b556 subunit"
FT /id="PRO_0000203515"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 27..52
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 53..68
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 90..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_note="ligand shared with second transmembrane
FT subunit"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
SQ SEQUENCE 129 AA; 14330 MW; 6394CEEA32C348A1 CRC64;
MIRNVKKQRP VNLDLQTIRF PITAIASILH RVSGVITFIA VGILLWLLGT SLSSPEGFQQ
AADIMDGFIV KFIMWGILTA LAYHVIVGIR HMLMDFGYLE ETFEAGQRSA KISFVITVVL
SLLAGVLVW
