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Database: UniProt
Entry: A0A1C2HQ62_9RHOB
LinkDB: A0A1C2HQ62_9RHOB
Original site: A0A1C2HQ62_9RHOB 
ID   A0A1C2HQ62_9RHOB        Unreviewed;       130 AA.
AC   A0A1C2HQ62;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Succinate dehydrogenase {ECO:0000313|EMBL:OCX65882.1};
GN   ORFNames=BFP70_07015 {ECO:0000313|EMBL:OCX65882.1};
OS   Thioclava sp. SK-1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1889770 {ECO:0000313|EMBL:OCX65882.1, ECO:0000313|Proteomes:UP000094269};
RN   [1] {ECO:0000313|EMBL:OCX65882.1, ECO:0000313|Proteomes:UP000094269}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-1 {ECO:0000313|EMBL:OCX65882.1,
RC   ECO:0000313|Proteomes:UP000094269};
RA   Wong S.-K., Hamasaki K., Yoshizawa S.;
RT   "Draft genome of Thioclava sp. strain SK-1.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC       {ECO:0000256|ARBA:ARBA00004050}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OCX65882.1}.
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DR   EMBL; MDHA01000032; OCX65882.1; -; Genomic_DNA.
DR   RefSeq; WP_066010640.1; NZ_MDHA01000032.1.
DR   AlphaFoldDB; A0A1C2HQ62; -.
DR   STRING; 1889770.BFP70_07015; -.
DR   OrthoDB; 9809280at2; -.
DR   Proteomes; UP000094269; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   CDD; cd03495; SQR_TypeC_SdhD_like; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE   4: Predicted;
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094269};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        24..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   130 AA;  14084 MW;  072ED69188C8F431 CRC64;
     MRYMTDRQRA VGKGASGTGT EHHWFMTISG VGLAFLVPCF VYIFGSALGR PQAEVIERLS
     HPFAAIVIAL TFLVGMRHFA KGAQSMIEDY AAGTTRKILV IFVYSLSYVL SAATLFALGK
     MVLMGLMASA
//
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