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Database: UniProt
Entry: A6T6F0_KLEP7
LinkDB: A6T6F0_KLEP7
Original site: A6T6F0_KLEP7 
ID   A6T6F0_KLEP7            Unreviewed;        91 AA.
AC   A6T6F0;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Succinate dehydrogenase cytochrome b556 subunit {ECO:0000256|ARBA:ARBA00020076};
GN   Name=sdhC {ECO:0000313|EMBL:ABR76171.1};
GN   ORFNames=KPN_00728 {ECO:0000313|EMBL:ABR76171.1};
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR76171.1, ECO:0000313|Proteomes:UP000000265};
RN   [1] {ECO:0000313|EMBL:ABR76171.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2] {ECO:0000313|EMBL:ABR76171.1, ECO:0000313|Proteomes:UP000000265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) 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; CP000647; ABR76171.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6T6F0; -.
DR   STRING; 272620.KPN_00728; -.
DR   PaxDb; 272620-KPN_00728; -.
DR   EnsemblBacteria; ABR76171; ABR76171; KPN_00728.
DR   KEGG; kpn:KPN_00728; -.
DR   HOGENOM; CLU_094691_2_2_6; -.
DR   Proteomes; UP000000265; 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: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   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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        72..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         46
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   91 AA;  9951 MW;  0D99B52259C1C211 CRC64;
     MAVGILLWLL GTSLSSPEGF LTAASIMDSF FVKFIMWGIL TALAYHVVVG IRHLMMDFGY
     LDETLEAGKR SAKISFVITV VLSLLAGVLV W
//
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