ID   DHSD_RICBR              Reviewed;         125 AA.
AC   Q1RHB6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN   Name=sdhD; OrderedLocusNames=RBE_1167;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05248.1; -; Genomic_DNA.
DR   RefSeq; WP_011477826.1; NC_007940.1.
DR   AlphaFoldDB; Q1RHB6; -.
DR   SMR; Q1RHB6; -.
DR   STRING; 336407.RBE_1167; -.
DR   EnsemblBacteria; ABE05248; ABE05248; RBE_1167.
DR   KEGG; rbe:RBE_1167; -.
DR   eggNOG; COG2142; Bacteria.
DR   HOGENOM; CLU_151315_0_2_5; -.
DR   OMA; MKLGMQV; -.
DR   OrthoDB; 2048140at2; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000001951; 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   PANTHER; PTHR38689; PTHR38689; 1.
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..125
FT                   /note="Succinate dehydrogenase hydrophobic membrane anchor
FT                   subunit"
FT                   /id="PRO_0000280979"
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..67
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        68..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        90..99
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        100..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
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         92
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   125 AA;  14208 MW;  90F259296FE3E721 CRC64;
     MTYDFRAEIV KAKNTGSAKS GSHHWLLQRI TAIILVLCSL WLLYFTLANK NSDVNIIIWE
     LKRPINLIPL LIAVITSLYH AMLGMQVVIE DYISCNKLRN TLIIAVKLFS ILTIVAFIVA
     VFYRG