DHSC_SALTY
ID DHSC_SALTY Reviewed; 129 AA.
AC P63725; Q8XG40;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Succinate dehydrogenase cytochrome b556 subunit;
DE Short=Cytochrome b-556;
GN Name=sdhC; OrderedLocusNames=STM0732;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE006468; AAL19676.1; -; Genomic_DNA.
DR RefSeq; NP_459717.1; NC_003197.2.
DR RefSeq; WP_001539490.1; NC_003197.2.
DR AlphaFoldDB; P63725; -.
DR SMR; P63725; -.
DR STRING; 99287.STM0732; -.
DR PaxDb; P63725; -.
DR EnsemblBacteria; AAL19676; AAL19676; STM0732.
DR GeneID; 1252252; -.
DR KEGG; stm:STM0732; -.
DR PATRIC; fig|99287.12.peg.764; -.
DR HOGENOM; CLU_094691_2_1_6; -.
DR OMA; YHLVAGI; -.
DR PhylomeDB; P63725; -.
DR BioCyc; SENT99287:STM0732-MON; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT CHAIN 1..129
FT /note="Succinate dehydrogenase cytochrome b556 subunit"
FT /id="PRO_0000203516"
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
