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Database: UniProt
Entry: A0A1N7NSR3_9RHOB
LinkDB: A0A1N7NSR3_9RHOB
Original site: A0A1N7NSR3_9RHOB 
ID   A0A1N7NSR3_9RHOB        Unreviewed;       131 AA.
AC   A0A1N7NSR3;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Succinate dehydrogenase cytochrome b556 subunit {ECO:0000256|ARBA:ARBA00020076};
GN   ORFNames=SAMN05421774_104109 {ECO:0000313|EMBL:SIT01403.1};
OS   Gemmobacter megaterium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Gemmobacter.
OX   NCBI_TaxID=1086013 {ECO:0000313|EMBL:SIT01403.1, ECO:0000313|Proteomes:UP000186141};
RN   [1] {ECO:0000313|EMBL:SIT01403.1, ECO:0000313|Proteomes:UP000186141}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26375 {ECO:0000313|EMBL:SIT01403.1,
RC   ECO:0000313|Proteomes:UP000186141};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) 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|PIRSR:PIRSR000178-1};
CC       Note=The heme is bound between the two transmembrane subunits.
CC       {ECO:0000256|PIRSR:PIRSR000178-1};
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. The complex can form homotrimers.
CC       {ECO:0000256|ARBA:ARBA00025912}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cytochrome b560 family.
CC       {ECO:0000256|ARBA:ARBA00007244}.
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DR   EMBL; FTOT01000004; SIT01403.1; -; Genomic_DNA.
DR   RefSeq; WP_076531306.1; NZ_FTOT01000004.1.
DR   AlphaFoldDB; A0A1N7NSR3; -.
DR   STRING; 1086013.SAMN05421774_104109; -.
DR   OrthoDB; 9799441at2; -.
DR   Proteomes; UP000186141; Unassembled WGS sequence.
DR   GO; GO:0045281; C:succinate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; 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:InterPro.
DR   CDD; cd03499; SQR_TypeC_SdhC; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR018495; Succ_DH_cyt_bsu_CS.
DR   InterPro; IPR014314; Succ_DH_cytb556.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   NCBIfam; TIGR02970; succ_dehyd_cytB; 1.
DR   PANTHER; PTHR10978; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT; 1.
DR   PANTHER; PTHR10978:SF5; SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT, MITOCHONDRIAL; 1.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   PIRSF; PIRSF000178; SDH_cyt_b560; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
DR   PROSITE; PS01001; SDH_CYT_2; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000178-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000178-1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000178-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186141};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022982}.
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         86
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:0000256|PIRSR:PIRSR000178-1"
SQ   SEQUENCE   131 AA;  14444 MW;  A7FC30C5F9A81E8E CRC64;
     MAEPKRVERP LSPFMIGPYY RPQMTSISSI MIRITGLALI VGIALIAAWI LSAAISEPAF
     DCVNWLVTSW LGWLVWIGSA WAIWYHLLGG VRHFIFDAGK AMDIPTAEKL GWAMFIGATV
     LTVITIIVAV V
//
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