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Database: UniProt
Entry: A0A1W6B0X5_9GAMM
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ID   A0A1W6B0X5_9GAMM        Unreviewed;       115 AA.
AC   A0A1W6B0X5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Succinate dehydrogenase hydrophobic membrane anchor subunit {ECO:0000256|ARBA:ARBA00019425, ECO:0000256|PIRNR:PIRNR000169};
GN   ORFNames=B1H58_01105 {ECO:0000313|EMBL:ARJ40732.1};
OS   Pantoea alhagi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=1891675 {ECO:0000313|EMBL:ARJ40732.1, ECO:0000313|Proteomes:UP000192900};
RN   [1] {ECO:0000313|EMBL:ARJ40732.1, ECO:0000313|Proteomes:UP000192900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LTYR-11Z {ECO:0000313|EMBL:ARJ40732.1,
RC   ECO:0000313|Proteomes:UP000192900};
RA   Zhang L.;
RT   "Complete genome sequence of the drought resistance-promoting endophyte
RT   Pantoea alhagi LTYR-11Z.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
CC       {ECO:0000256|ARBA:ARBA00004050, ECO:0000256|PIRNR:PIRNR000169}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000169-2};
CC       Note=The heme is bound between the two transmembrane subunits.
CC       {ECO:0000256|PIRSR:PIRSR000169-2};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC       {ECO:0000256|ARBA:ARBA00005163, ECO:0000256|PIRNR:PIRNR000169}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429, ECO:0000256|PIRNR:PIRNR000169}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004429,
CC       ECO:0000256|PIRNR:PIRNR000169}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP019706; ARJ40732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W6B0X5; -.
DR   STRING; 1891675.B1H58_01105; -.
DR   KEGG; palh:B1H58_01105; -.
DR   OrthoDB; 5612767at2; -.
DR   UniPathway; UPA00223; -.
DR   Proteomes; UP000192900; Chromosome.
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:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd03494; SQR_TypeC_SdhD; 1.
DR   Gene3D; 1.20.1300.10; Fumarate reductase/succinate dehydrogenase, transmembrane subunit; 1.
DR   InterPro; IPR034804; SQR/QFR_C/D.
DR   InterPro; IPR014312; Succ_DH_anchor.
DR   InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR   NCBIfam; TIGR02968; succ_dehyd_anc; 1.
DR   PANTHER; PTHR38689; SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR SUBUNIT; 1.
DR   PANTHER; PTHR38689:SF1; SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR SUBUNIT; 1.
DR   Pfam; PF01127; Sdh_cyt; 1.
DR   PIRSF; PIRSF000169; SDH_D; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
PE   4: Predicted;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW   ECO:0000256|PIRNR:PIRNR000169};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR000169};
KW   Electron transport {ECO:0000256|PIRNR:PIRNR000169};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000169-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000169-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000169};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR000169-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192900};
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|PIRNR:PIRNR000169};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR000169}.
FT   TRANSMEM        17..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        92..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         71
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:PIRSR000169-2"
FT   BINDING         83
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000169-1"
SQ   SEQUENCE   115 AA;  13020 MW;  CC9E03777F5B6A57 CRC64;
     MVSNATALGR NGVQDWLLLR ATAILITLYT LYILGFIIVS DTLTYDIWRA FFASSFTKVF
     TLLTLFSTVI HGWIGMWQVL TDYVKPLAWR LLLQLVIVVT LLVYAIYGTV VVWGA
//
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