SDHC_MYCTU
ID SDHC_MYCTU Reviewed; 136 AA.
AC O53368; I6XGV7; Q7D5Q4;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Succinate dehydrogenase 2 membrane subunit SdhC {ECO:0000305};
GN Name=sdhC {ECO:0000312|EMBL:CCP46136.1};
GN OrderedLocusNames=Rv3316 {ECO:0000312|EMBL:CCP46136.1},
GN RVBD_3316 {ECO:0000312|EMBL:AFN51324.1};
GN ORFNames=P425_03457 {ECO:0000312|EMBL:KBJ28045.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genome Sequencing Platform;
RA Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 2-10, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=H37Rv;
RX PubMed=25412183; DOI=10.1371/journal.ppat.1004510;
RA Hartman T., Weinrick B., Vilcheze C., Berney M., Tufariello J., Cook G.M.,
RA Jacobs W.R. Jr.;
RT "Succinate dehydrogenase is the regulator of respiration in Mycobacterium
RT tuberculosis.";
RL PLoS Pathog. 10:E1004510-E1004510(2014).
CC -!- FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase 2
CC (Sdh2). Sdh2 may catalyze the two-electron oxidation of succinate to
CC fumarate with a corresponding reduction of quinone to quinol under low
CC oxygen conditions, when the primary aerobic succinate dehydrogenase
CC (Sdh1) is inhibited. Sdh2 seems to be the generator of the proton
CC motive force (PMF) under hypoxia. {ECO:0000305|PubMed:25412183}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P69054};
CC Note=The heme is bound between the two transmembrane subunits.
CC {ECO:0000250|UniProtKB:P69054};
CC -!- SUBUNIT: Part of an enzyme complex containing four subunits: a
CC flavoprotein (SdhA), an iron-sulfur protein (SdhB), plus two membrane-
CC anchoring proteins (SdhC and SdhD). {ECO:0000305|PubMed:25412183}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking the sdh2 operon (sdhCDAB) display a
CC stationary phase exit defect after 60 days in culture. They show only
CC slight difference in intracellular succinate and malate concentrations
CC during aerobic growth or hypoxia when compared to wild-type. The mutant
CC strain is more susceptible to proton motive force (PMF) inhibition than
CC the parental strain, and it was impossible to recover colonies from
CC mutant cultures after 21 days. Cells harboring a deletion of sdh2
CC consume oxygen at a reduced rate and are able to modulate respiration
CC as dissolved oxygen (DO) is depleted to about 6%.
CC {ECO:0000269|PubMed:25412183}.
CC -!- SIMILARITY: Belongs to the cytochrome b560 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AFN51324.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
CC Sequence=CCP46136.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
CC Sequence=KBJ28045.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP46136.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP003248; AFN51324.1; ALT_INIT; Genomic_DNA.
DR EMBL; JLDD01000040; KBJ28045.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_217833.1; NC_000962.3.
DR RefSeq; WP_003900017.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; O53368; -.
DR SMR; O53368; -.
DR STRING; 83332.Rv3316; -.
DR PaxDb; O53368; -.
DR DNASU; 887969; -.
DR GeneID; 45427316; -.
DR GeneID; 887969; -.
DR KEGG; mtu:Rv3316; -.
DR KEGG; mtv:RVBD_3316; -.
DR PATRIC; fig|83332.111.peg.3701; -.
DR TubercuList; Rv3316; -.
DR eggNOG; COG2009; Bacteria.
DR HOGENOM; CLU_127125_0_1_11; -.
DR BioCyc; MetaCyc:G185E-7591-MON; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:UniProtKB-KW.
DR Gene3D; 1.20.1300.10; -; 1.
DR InterPro; IPR039023; SdhC_prok.
DR InterPro; IPR034804; SQR/QFR_C/D.
DR InterPro; IPR014314; Succ_DH_cytb556.
DR InterPro; IPR000701; SuccDH_FuR_B_TM-su.
DR PANTHER; PTHR41910; PTHR41910; 1.
DR Pfam; PF01127; Sdh_cyt; 1.
DR SUPFAM; SSF81343; SSF81343; 1.
DR TIGRFAMs; TIGR02970; succ_dehyd_cytB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:34915127"
FT CHAIN 2..136
FT /note="Succinate dehydrogenase 2 membrane subunit SdhC"
FT /id="PRO_0000432512"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 85
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:0000250|UniProtKB:P69054"
SQ SEQUENCE 136 AA; 15480 MW; E2FE3965D53F95D9 CRC64;
MNTTATTVSR GRRPPRTLYR GDPGMWSWVC HRISGATIFF FLFVHVLDAA MLRVSPQTYN
AVLATYKTPI VGLMEYGLVA AVLFHALNGI RVILIDFWSE GPRYQRLMLW IIGSVFLLLM
VPAGVVVGIH MWEHFR
