ID Q3YSR5_EHRCJ Unreviewed; 136 AA.
AC Q3YSR5;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Succinate dehydrogenase cytochrome b556 subunit {ECO:0000256|ARBA:ARBA00020076};
GN OrderedLocusNames=Ecaj_0189 {ECO:0000313|EMBL:AAZ68240.1};
OS Ehrlichia canis (strain Jake).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484 {ECO:0000313|EMBL:AAZ68240.1, ECO:0000313|Proteomes:UP000000435};
RN [1] {ECO:0000313|Proteomes:UP000000435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake {ECO:0000313|Proteomes:UP000000435};
RX PubMed=16707693; DOI=10.1128/JB.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(2006).
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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC {ECO:0000256|ARBA:ARBA00005163}.
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; CP000107; AAZ68240.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3YSR5; -.
DR STRING; 269484.Ecaj_0189; -.
DR KEGG; ecn:Ecaj_0189; -.
DR eggNOG; COG2009; Bacteria.
DR HOGENOM; CLU_094691_1_1_5; -.
DR InParanoid; Q3YSR5; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000000435; Chromosome.
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:UniProtKB-UniPathway.
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 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 Oxidoreductase {ECO:0000313|EMBL:AAZ68240.1};
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:ARBA00022448}.
FT TRANSMEM 37..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 91
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 136 AA; 15975 MW; 6398ED57946594A7 CRC64;
MFHFFNLIMS KVRPLSPHLQ IYKVVYKLSI MHRFTGMLLF VGLFIISWGI IAAFLFPKII
YEIYNFFSTC YLALYSFKLI AFIWLNIFSY HYLNGIRHLL WDLGFCLTKS AVKVTGIIVV
CLCIISSFIL YSLFLS
//
