ID   DHSC_RICPR              Reviewed;         124 AA.
AC   P41085;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Succinate dehydrogenase cytochrome b556 subunit;
DE            Short=Cytochrome b-556;
GN   Name=sdhC; OrderedLocusNames=RP126;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Madrid E;
RA   Wood D.O.;
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; U02603; AAA18325.1; -; Unassigned_DNA.
DR   EMBL; AJ235270; CAA14595.1; -; Genomic_DNA.
DR   PIR; D71722; D71722.
DR   RefSeq; NP_220518.1; NC_000963.1.
DR   RefSeq; WP_004597166.1; NC_000963.1.
DR   AlphaFoldDB; P41085; -.
DR   SMR; P41085; -.
DR   STRING; 272947.RP126; -.
DR   EnsemblBacteria; CAA14595; CAA14595; CAA14595.
DR   GeneID; 57569254; -.
DR   KEGG; rpr:RP126; -.
DR   PATRIC; fig|272947.5.peg.128; -.
DR   eggNOG; COG2009; Bacteria.
DR   HOGENOM; CLU_094691_3_1_5; -.
DR   OMA; GYTWALM; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000002480; 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; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT   CHAIN           1..124
FT                   /note="Succinate dehydrogenase cytochrome b556 subunit"
FT                   /id="PRO_0000203514"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        30..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        56..67
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        89..103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   BINDING         83
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   124 AA;  14383 MW;  070111704551ACB6 CRC64;
     MTKIKQEIYN KRPTSPHLTI YKPQISSTLS ILHRMTGVAL FFVVSILVWW LILSKYDNNY
     LQLASCCIIK ICLVAFSYSW CYHLCNGIRH LFWDIGYGFS IKAVNITGWC VVVCSILLTM
     LLWV