DHSD_RICPR
ID DHSD_RICPR Reviewed; 125 AA.
AC P41086;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit;
GN Name=sdhD; OrderedLocusNames=RP127;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Madrid E;
RA Wood D.O.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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; U02603; AAA18326.1; -; Unassigned_DNA.
DR EMBL; AJ235270; CAA14596.1; -; Genomic_DNA.
DR PIR; E71722; E71722.
DR RefSeq; NP_220519.1; NC_000963.1.
DR RefSeq; WP_004597167.1; NC_000963.1.
DR AlphaFoldDB; P41086; -.
DR SMR; P41086; -.
DR STRING; 272947.RP127; -.
DR EnsemblBacteria; CAA14596; CAA14596; CAA14596.
DR GeneID; 57569255; -.
DR KEGG; rpr:RP127; -.
DR PATRIC; fig|272947.5.peg.129; -.
DR eggNOG; COG2142; Bacteria.
DR HOGENOM; CLU_151315_0_2_5; -.
DR OMA; MKLGMQV; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000002480; 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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT CHAIN 1..125
FT /note="Succinate dehydrogenase hydrophobic membrane anchor
FT subunit"
FT /id="PRO_0000158678"
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; 14555 MW; F7E60E6A1BB455D4 CRC64;
MIYDFKAEII KAKNSSFSKS GSHHWLLQRV TGVILALCSF WLIYFMFTNK NNDINIIMWE
FKKPFNIVIL LITVTISLYH SVLGMRVVIE DYINCHKLRN TLIIIVKLFC ILTIVSFVVA
IFYSG
