ID   DHSD_RICTY              Reviewed;         125 AA.
AC   Q68XP0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN   Name=sdhD; OrderedLocusNames=RT0116;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03602.1; -; Genomic_DNA.
DR   RefSeq; WP_011190589.1; NC_006142.1.
DR   AlphaFoldDB; Q68XP0; -.
DR   SMR; Q68XP0; -.
DR   STRING; 257363.RT0116; -.
DR   EnsemblBacteria; AAU03602; AAU03602; RT0116.
DR   KEGG; rty:RT0116; -.
DR   eggNOG; COG2142; Bacteria.
DR   HOGENOM; CLU_151315_0_2_5; -.
DR   OMA; MKLGMQV; -.
DR   OrthoDB; 2048140at2; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000000604; 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_0000280981"
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;  14523 MW;  E706A13E55B89704 CRC64;
     MIYDFKAEII KSKSSSSSKS GAHHWLLQRV TGVVLALCSF WLIYFMFTNK NNDINIIMWE
     FKKPFNIVIL LITVTISLYH SVLGMRVVIE DYINCHKLRN TLIIIVKLFC ILTIVAFIVA
     IFYSE