DHSD_COXBU
ID DHSD_COXBU Reviewed; 115 AA.
AC P51057;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN Name=sdhD; OrderedLocusNames=CBU_1402;
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], FUNCTION, AND SUBUNIT.
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 {ECO:0000269|PubMed:7698664}.
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. {ECO:0000269|PubMed:7698664}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA74132.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L33409; AAA74132.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE016828; AAO90901.2; -; Genomic_DNA.
DR PIR; I40848; I40848.
DR RefSeq; NP_820387.2; NC_002971.3.
DR RefSeq; WP_010958203.1; NC_002971.4.
DR AlphaFoldDB; P51057; -.
DR SMR; P51057; -.
DR STRING; 227377.CBU_1402; -.
DR PRIDE; P51057; -.
DR EnsemblBacteria; AAO90901; AAO90901; CBU_1402.
DR GeneID; 1209308; -.
DR KEGG; cbu:CBU_1402; -.
DR PATRIC; fig|227377.7.peg.1404; -.
DR eggNOG; COG2142; Bacteria.
DR HOGENOM; CLU_151315_2_0_6; -.
DR OMA; QWMKVLT; -.
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:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000104; F:succinate dehydrogenase activity; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0017004; P:cytochrome complex assembly; IBA:GO_Central.
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; IPR014312; Succ_DH_anchor.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR PANTHER; PTHR38689; PTHR38689; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR PIRSF; PIRSF000169; SDH_D; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR TIGRFAMs; TIGR02968; succ_dehyd_anc; 1.
PE 1: Evidence at protein level;
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..115
FT /note="Succinate dehydrogenase hydrophobic membrane anchor
FT subunit"
FT /id="PRO_0000158671"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 36..57
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 80..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 90..113
FT /note="Helical"
FT /evidence="ECO:0000250"
FT BINDING 70
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"
FT BINDING 82
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
SQ SEQUENCE 115 AA; 13774 MW; BCBC16AE4DFCC180 CRC64;
MDMVDRTSRR GYRDWFVQRI TALLSGIYAV FVIVFLLVHH PISYPQWHAL FSHLIMKIFT
LIVIFSILWH AWIGMWTIFT DYVKNKPIRL ALETLVCLLL VGYFVWAIEF LWIAR
