ID   QCR2_KLULA              Reviewed;         360 AA.
AC   Q6CWJ6;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial;
DE   AltName: Full=Complex III subunit 2;
DE   AltName: Full=Core protein II;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 2;
DE   Flags: Precursor;
GN   Name=QCR2; OrderedLocusNames=KLLA0B03564g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a
CC       multisubunit transmembrane complex that is part of the mitochondrial
CC       electron transport chain which drives oxidative phosphorylation. The
CC       respiratory chain contains 3 multisubunit complexes succinate
CC       dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase
CC       (complex IV, CIV), that cooperate to transfer electrons derived from
CC       NADH and succinate to molecular oxygen, creating an electrochemical
CC       gradient over the inner membrane that drives transmembrane transport
CC       and the ATP synthase. The cytochrome b-c1 complex catalyzes electron
CC       transfer from ubiquinol to cytochrome c, linking this redox reaction to
CC       translocation of protons across the mitochondrial inner membrane, with
CC       protons being carried across the membrane as hydrogens on the quinol.
CC       In the process called Q cycle, 2 protons are consumed from the matrix,
CC       4 protons are released into the intermembrane space and 2 electrons are
CC       passed to cytochrome c. {ECO:0000250|UniProtKB:P07257}.
CC   -!- SUBUNIT: Component of the ubiquinol-cytochrome c oxidoreductase
CC       (cytochrome b-c1 complex, complex III, CIII), a multisubunit enzyme
CC       composed of 3 respiratory subunits cytochrome b, cytochrome c1 and
CC       Rieske protein, 2 core protein subunits, and additional low-molecular
CC       weight protein subunits. The complex exists as an obligatory dimer and
CC       forms supercomplexes (SCs) in the inner mitochondrial membrane with
CC       cytochrome c oxidase (complex IV, CIV). {ECO:0000250|UniProtKB:P07257}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P07257}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P07257}; Matrix side
CC       {ECO:0000250|UniProtKB:P07257}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Does not seem to have protease activity as it lacks the zinc-
CC       binding site. {ECO:0000305}.
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DR   EMBL; CR382122; CAH02086.1; -; Genomic_DNA.
DR   RefSeq; XP_451693.1; XM_451693.1.
DR   AlphaFoldDB; Q6CWJ6; -.
DR   SMR; Q6CWJ6; -.
DR   STRING; 284590.Q6CWJ6; -.
DR   PaxDb; 284590-Q6CWJ6; -.
DR   GeneID; 2897081; -.
DR   KEGG; kla:KLLA0_B03564g; -.
DR   eggNOG; KOG2583; Eukaryota.
DR   HOGENOM; CLU_009902_0_1_1; -.
DR   InParanoid; Q6CWJ6; -.
DR   OMA; YKYQDAG; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF209; CYTOCHROME B-C1 COMPLEX SUBUNIT 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Reference proteome; Respiratory chain; Transit peptide; Transport.
FT   TRANSIT         1..15
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           16..360
FT                   /note="Cytochrome b-c1 complex subunit 2, mitochondrial"
FT                   /id="PRO_0000026797"
SQ   SEQUENCE   360 AA;  39248 MW;  0E5B9D6D6AB18A4A CRC64;
     MLSSRLQFAQ QTARKFSISA KDGSGKLSTL AVKVHGGSRY ADKEGIAHLL SRFNFHNTGN
     KSALRLVRES ELLGGKFESS VDREYITLKA TFLKEDLPYF VNALGNVLYK TSFRPHELPE
     SVLPAAKYDI SVSETNPINK AEDLLYNVSF RKDLGNTVLY RGVEKVTLDD IKAYANKVYT
     KENIEIVGQG VNEADLKRFV NDSLIGSLPT GSKLAAQAQP KFFSGEARLS APGASVAAIA
     VPVTKEQFAT YEVLAKYLTS ALSELSPLID SAKLDKYANA GLFSLYVKGE DASVVAENIK
     KVVDTLKKDV DISAAKEYTA LQLSLENAPI DVSNVKNVKL DKFSYAAVGN VAKLPFADEL
//