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Database: UniProt
Entry: H3RAS2_PANSE
LinkDB: H3RAS2_PANSE
Original site: H3RAS2_PANSE 
ID   H3RAS2_PANSE            Unreviewed;        65 AA.
AC   H3RAS2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Succinate dehydrogenase cytochrome b556 subunit {ECO:0000256|ARBA:ARBA00020076};
GN   ORFNames=CKS_3784 {ECO:0000313|EMBL:EHU01522.1};
OS   Pantoea stewartii subsp. stewartii DC283.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=660596 {ECO:0000313|EMBL:EHU01522.1, ECO:0000313|Proteomes:UP000005050};
RN   [1] {ECO:0000313|EMBL:EHU01522.1, ECO:0000313|Proteomes:UP000005050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC283 {ECO:0000313|EMBL:EHU01522.1,
RC   ECO:0000313|Proteomes:UP000005050};
RX   PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA   Wang X., Yang F., von Bodman S.B.;
RT   "The genetic and structural basis of two distinct terminal side branch
RT   residues in stewartan and amylovoran exopolysaccharides and their potential
RT   role in host adaptation.";
RL   Mol. Microbiol. 83:195-207(2012).
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   -!- 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}.
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:EHU01522.1}.
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DR   EMBL; AHIE01000004; EHU01522.1; -; Genomic_DNA.
DR   AlphaFoldDB; H3RAS2; -.
DR   SMR; H3RAS2; -.
DR   STRING; 660596.DSJ_08300; -.
DR   PATRIC; fig|660596.6.peg.1057; -.
DR   eggNOG; COG2009; Bacteria.
DR   Proteomes; UP000005050; 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:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; 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   Pfam; PF01127; Sdh_cyt; 1.
DR   SUPFAM; SSF81343; Fumarate reductase respiratory complex transmembrane subunits; 1.
DR   PROSITE; PS01001; SDH_CYT_2; 1.
PE   3: Inferred from homology;
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   Oxidoreductase {ECO:0000313|EMBL:EHU01522.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   65 AA;  7137 MW;  AFF13D7ED1E476E5 CRC64;
     MSGFFVKFIM WGILTALAYH TVGGIRHMLM DFGYLAETLE AGKRSAQVTF GITVVLSILA
     GVLVW
//
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