DHSC_ECOLI
ID DHSC_ECOLI Reviewed; 129 AA.
AC P69054; P10446;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Succinate dehydrogenase cytochrome b556 subunit;
DE Short=Cytochrome b-556;
GN Name=sdhC; Synonyms=cybA; OrderedLocusNames=b0721, JW0711;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6383359; DOI=10.1042/bj2220519;
RA Wood D., Darlison M.G., Wilde R.J., Guest J.R.;
RT "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of
RT the succinate dehydrogenase of Escherichia coli.";
RL Biochem. J. 222:519-534(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3309132; DOI=10.1099/00221287-132-12-3239;
RA Wilde R.J., Guest J.R.;
RT "Transcript analysis of the citrate synthase and succinate dehydrogenase
RT genes of Escherichia coli K12.";
RL J. Gen. Microbiol. 132:3239-3251(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 17-33, AND MUTAGENESIS.
RC STRAIN=K12;
RX PubMed=9822661; DOI=10.1074/jbc.273.48.31916;
RA Yang X., Yu L., He D., Yu C.-A.;
RT "The quinone-binding site in succinate-ubiquinone reductase from
RT Escherichia coli. Quinone-binding domain and amino acid residues involved
RT in quinone binding.";
RL J. Biol. Chem. 273:31916-31923(1998).
RN [7]
RP IDENTIFICATION OF PROTEIN.
RA Murakami H., Kika K., Oya H., Anraku Y.;
RT "The Escherichia coli cytochrome b556 gene, cybA is assignable as sdhC in
RT the succinate dehydrogenase gene cluster.";
RL FEMS Microbiol. Lett. 30:307-311(1985).
RN [8]
RP MUTAGENESIS OF HISTIDINE RESIDUES.
RX PubMed=9521736; DOI=10.1021/bi9716635;
RA Vibat C.R., Cecchini G., Nakamura K., Kita K., Gennis R.B.;
RT "Localization of histidine residues responsible for heme axial ligation in
RT cytochrome b556 of complex II (succinate:ubiquinone oxidoreductase) in
RT Escherichia coli.";
RL Biochemistry 37:4148-4159(1998).
RN [9]
RP MUTAGENESIS OF HISTIDINE RESIDUES.
RX PubMed=11259408; DOI=10.1074/jbc.m011270200;
RA Maklashina E., Rothery R.A., Weiner J.H., Cecchini G.;
RT "Retention of heme in axial ligand mutants of succinate-ubiquinone
RT oxidoreductase (complex II) from Escherichia coli.";
RL J. Biol. Chem. 276:18968-18976(2001).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH HEME, TRANSMEMBRANE
RP TOPOLOGY, AND SUBUNIT.
RX PubMed=12560550; DOI=10.1126/science.1079605;
RA Yankovskaya V., Horsefield R., Toernroth S., Luna-Chavez C., Miyoshi H.,
RA Leger C., Byrne B., Cecchini G., Iwata S.;
RT "Architecture of succinate dehydrogenase and reactive oxygen species
RT generation.";
RL Science 299:700-704(2003).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH HEME, TRANSMEMBRANE
RP TOPOLOGY, AND SUBUNIT.
RX PubMed=16407191; DOI=10.1074/jbc.m508173200;
RA Horsefield R., Yankovskaya V., Sexton G., Whittingham W., Shiomi K.,
RA Omura S., Byrne B., Cecchini G., Iwata S.;
RT "Structural and computational analysis of the quinone-binding site of
RT complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron
RT transfer and proton conduction during ubiquinone reduction.";
RL J. Biol. Chem. 281:7309-7316(2006).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH HEME, TRANSMEMBRANE
RP TOPOLOGY, AND SUBUNIT.
RX PubMed=19710024; DOI=10.1074/jbc.m109.010058;
RA Ruprecht J., Yankovskaya V., Maklashina E., Iwata S., Cecchini G.;
RT "Structure of Escherichia coli succinate:quinone oxidoreductase with an
RT occupied and empty quinone-binding site.";
RL J. Biol. Chem. 284:29836-29846(2009).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=The heme is bound between the two transmembrane subunits.;
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.
CC {ECO:0000269|PubMed:12560550, ECO:0000269|PubMed:16407191,
CC ECO:0000269|PubMed:19710024}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: His-84 provides an axial ligand to heme b556 in the
CC wild-type enzyme. The retention of low spin heme b556 in the SdhC 'Leu-
CC 84' mutant suggests that swapping of the heme axial ligand by His-91 or
CC His-30 is possible.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
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DR EMBL; J01619; AAA23893.1; -; Genomic_DNA.
DR EMBL; M28989; AAA24616.1; -; Genomic_DNA.
DR EMBL; X00980; CAA25485.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73815.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35388.1; -; Genomic_DNA.
DR PIR; A28836; DEECS4.
DR RefSeq; NP_415249.1; NC_000913.3.
DR RefSeq; WP_001308496.1; NZ_CP047127.1.
DR PDB; 1NEK; X-ray; 2.60 A; C=1-129.
DR PDB; 1NEN; X-ray; 2.90 A; C=1-129.
DR PDB; 2ACZ; X-ray; 3.10 A; C=1-129.
DR PDB; 2WDQ; X-ray; 2.40 A; C/G/K=1-129.
DR PDB; 2WDR; X-ray; 3.20 A; C/G/K=1-129.
DR PDB; 2WDV; X-ray; 3.20 A; C/G/K=1-129.
DR PDB; 2WP9; X-ray; 2.70 A; C/G/K=1-129.
DR PDB; 2WS3; X-ray; 3.20 A; C/G/K=1-129.
DR PDB; 2WU2; X-ray; 2.50 A; C/G/K=1-129.
DR PDB; 2WU5; X-ray; 2.80 A; C/G/K=1-129.
DR PDB; 6WU6; EM; 3.60 A; C/G/K=1-129.
DR PDB; 7JZ2; EM; 2.50 A; C/G/K=1-129.
DR PDBsum; 1NEK; -.
DR PDBsum; 1NEN; -.
DR PDBsum; 2ACZ; -.
DR PDBsum; 2WDQ; -.
DR PDBsum; 2WDR; -.
DR PDBsum; 2WDV; -.
DR PDBsum; 2WP9; -.
DR PDBsum; 2WS3; -.
DR PDBsum; 2WU2; -.
DR PDBsum; 2WU5; -.
DR PDBsum; 6WU6; -.
DR PDBsum; 7JZ2; -.
DR AlphaFoldDB; P69054; -.
DR SMR; P69054; -.
DR BioGRID; 4259942; 36.
DR BioGRID; 849692; 1.
DR ComplexPortal; CPX-1931; Respiratory chain complex II.
DR DIP; DIP-10837N; -.
DR IntAct; P69054; 4.
DR STRING; 511145.b0721; -.
DR DrugBank; DB07671; 2-[1-METHYLHEXYL]-4,6-DINITROPHENOL.
DR DrugBank; DB04631; Atpenin A5.
DR DrugBank; DB08690; Ubiquinone Q2.
DR jPOST; P69054; -.
DR PaxDb; P69054; -.
DR PRIDE; P69054; -.
DR EnsemblBacteria; AAC73815; AAC73815; b0721.
DR EnsemblBacteria; BAA35388; BAA35388; BAA35388.
DR GeneID; 945316; -.
DR KEGG; ecj:JW0711; -.
DR KEGG; eco:b0721; -.
DR PATRIC; fig|511145.12.peg.751; -.
DR EchoBASE; EB0926; -.
DR eggNOG; COG2009; Bacteria.
DR HOGENOM; CLU_094691_2_1_6; -.
DR InParanoid; P69054; -.
DR OMA; YHLVAGI; -.
DR PhylomeDB; P69054; -.
DR BioCyc; EcoCyc:SDH-MEMB1; -.
DR BioCyc; MetaCyc:SDH-MEMB1; -.
DR UniPathway; UPA00223; -.
DR EvolutionaryTrace; P69054; -.
DR PHI-base; PHI:7962; -.
DR PRO; PR:P69054; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0045281; C:succinate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IDA:EcoCyc.
DR GO; GO:0020037; F:heme binding; IMP:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008177; F:succinate dehydrogenase (ubiquinone) activity; IMP:EcoliWiki.
DR GO; GO:0048039; F:ubiquinone binding; IDA:EcoliWiki.
DR GO; GO:0009060; P:aerobic respiration; IEP:EcoCyc.
DR GO; GO:0017004; P:cytochrome complex assembly; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Tricarboxylic acid cycle.
FT CHAIN 1..129
FT /note="Succinate dehydrogenase cytochrome b556 subunit"
FT /id="PRO_0000203510"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 27..52
FT /note="Helical"
FT TOPO_DOM 53..68
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 69..89
FT /note="Helical"
FT TOPO_DOM 90..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 109..129
FT /note="Helical"
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 HELIX 15..17
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 22..52
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 55..66
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 68..95
FT /evidence="ECO:0007829|PDB:2WDQ"
FT HELIX 103..126
FT /evidence="ECO:0007829|PDB:2WDQ"
SQ SEQUENCE 129 AA; 14299 MW; 57485D25D2535818 CRC64;
MIRNVKKQRP VNLDLQTIRF PITAIASILH RVSGVITFVA VGILLWLLGT SLSSPEGFEQ
ASAIMGSFFV KFIMWGILTA LAYHVVVGIR HMMMDFGYLE ETFEAGKRSA KISFVITVVL
SLLAGVLVW
