DHSD_RICCN
ID DHSD_RICCN Reviewed; 126 AA.
AC Q92J98;
DT 11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN Name=sdhD; OrderedLocusNames=RC0169;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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DR EMBL; AE006914; AAL02707.1; -; Genomic_DNA.
DR PIR; A97721; A97721.
DR RefSeq; WP_010976844.1; NC_003103.1.
DR AlphaFoldDB; Q92J98; -.
DR SMR; Q92J98; -.
DR EnsemblBacteria; AAL02707; AAL02707; RC0169.
DR KEGG; rco:RC0169; -.
DR HOGENOM; CLU_151315_0_2_5; -.
DR OMA; MKLGMQV; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000000816; 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:0020037; F:heme binding; 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; IPR014312; Succ_DH_anchor.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR Pfam; PF01127; Sdh_cyt; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR TIGRFAMs; TIGR02968; succ_dehyd_anc; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Transmembrane; Transmembrane helix; Transport;
KW Tricarboxylic acid cycle.
FT CHAIN 1..126
FT /note="Succinate dehydrogenase hydrophobic membrane anchor
FT subunit"
FT /id="PRO_0000158677"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 46..68
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 69..90
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 91..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 101..124
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"
FT BINDING 93
FT /ligand="a ubiquinone"
FT /ligand_id="ChEBI:CHEBI:16389"
FT /evidence="ECO:0000250"
SQ SEQUENCE 126 AA; 14403 MW; 72B93A63BF0B2C13 CRC64;
MVYDFKAEIV KAKNSGSAKS GSHHWLLQRV TGIILALCSV WLIYFTLTNK NNDINIIMLW
ELKKPFNVVA LLITVVISLY HAMLGMRVVI EDYISYHKLR NTLIIIVQLF CIVTIVAFVV
ALFYKG
