DHSC_COXBU
ID DHSC_COXBU Reviewed; 125 AA.
AC P51055;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Succinate dehydrogenase cytochrome b556 subunit;
DE Short=Cytochrome b-556;
GN Name=sdhC; OrderedLocusNames=CBU_1403;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nine Mile;
RX PubMed=7698664; DOI=10.1016/0378-1119(94)00888-y;
RA Heinzen R.A., Mo Y.-Y., Robertson S.J., Mallavia L.P.;
RT "Characterization of the succinate dehydrogenase-encoding gene cluster
RT (sdh) from the rickettsia Coxiella burnetii.";
RL Gene 155:27-34(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAO90902.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L33409; AAA74131.1; -; Genomic_DNA.
DR EMBL; AE016828; AAO90902.2; ALT_INIT; Genomic_DNA.
DR PIR; I40847; I40847.
DR RefSeq; NP_820388.2; NC_002971.3.
DR AlphaFoldDB; P51055; -.
DR SMR; P51055; -.
DR STRING; 227377.CBU_1403; -.
DR EnsemblBacteria; AAO90902; AAO90902; CBU_1403.
DR GeneID; 1209309; -.
DR KEGG; cbu:CBU_1403; -.
DR PATRIC; fig|227377.7.peg.1405; -.
DR eggNOG; COG2009; Bacteria.
DR HOGENOM; CLU_094691_2_1_6; -.
DR OMA; SWAFLHH; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000002671; 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..125
FT /note="Succinate dehydrogenase cytochrome b556 subunit"
FT /id="PRO_0000203509"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 23..48
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 49..65
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 87..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000250"
FT BINDING 81
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 125 AA; 14311 MW; 7200237283074FF8 CRC64;
MNAKRPVNLD LTKFHFPPMA ILSIGHRISG FVLFLCMPLM FYLLHRATAS AESFYHLHQL
LLHNGWIKLA VWIMLSATLF HLFAGIRHLA MDLGFWESVP EGRISAYTVF VVSFIAIVLA
GVWIW