QCRB_BACSU
ID QCRB_BACSU Reviewed; 224 AA.
AC P46912;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Menaquinol-cytochrome c reductase cytochrome b subunit;
GN Name=qcrB; Synonyms=bfcB; OrderedLocusNames=BSU22550;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BR151;
RX PubMed=7592464; DOI=10.1128/jb.177.23.6751-6760.1995;
RA Yu J., Hederstedt L., Piggot P.J.;
RT "The cytochrome bc complex (menaquinone:cytochrome c reductase) in Bacillus
RT subtilis has a nontraditional subunit organization.";
RL J. Bacteriol. 177:6751-6760(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8760912; DOI=10.1099/13500872-142-8-2005;
RA Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D.,
RA Serror P.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT serA and kdg loci cloned in a yeast artificial chromosome.";
RL Microbiology 142:2005-2016(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP HEME-BINDING.
RX PubMed=9535866; DOI=10.1074/jbc.273.15.8860;
RA Yu J., Le Brun N.E.;
RT "Studies of the cytochrome subunits of menaquinone:cytochrome c reductase
RT (bc complex) of Bacillus subtilis. Evidence for the covalent attachment of
RT heme to the cytochrome b subunit.";
RL J. Biol. Chem. 273:8860-8866(1998).
CC -!- FUNCTION: Component of the menaquinol-cytochrome c reductase complex.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Note=Binds 2 heme groups per subunit. One heme group is bound
CC covalently by a single cysteine link, the other one non-covalently.;
CC -!- SUBUNIT: The main subunits of the menaquinone:cytochrome c complex are:
CC cytochrome b, the Rieske protein and a cytochrome b/c subunit.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: This cytochrome b is similar to other bacterial and
CC plant chloroplast cytochrome b6 proteins in binding one of two hemes
CC with a single thioether bond.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00968}.
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DR EMBL; U25535; AAA85561.1; -; Genomic_DNA.
DR EMBL; L47709; AAB38436.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14171.1; -; Genomic_DNA.
DR PIR; C69687; C69687.
DR RefSeq; NP_390136.1; NC_000964.3.
DR RefSeq; WP_003225560.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P46912; -.
DR SMR; P46912; -.
DR STRING; 224308.BSU22550; -.
DR TCDB; 3.D.3.4.1; the proton-translocating quinol:cytochrome c reductase (qcr) superfamily.
DR PaxDb; P46912; -.
DR EnsemblBacteria; CAB14171; CAB14171; BSU_22550.
DR GeneID; 23410288; -.
DR GeneID; 64304035; -.
DR GeneID; 939019; -.
DR KEGG; bsu:BSU22550; -.
DR PATRIC; fig|224308.179.peg.2459; -.
DR eggNOG; COG1290; Bacteria.
DR InParanoid; P46912; -.
DR OMA; WATQTGM; -.
DR PhylomeDB; P46912; -.
DR BioCyc; BSUB:BSU22550-MON; -.
DR BioCyc; MetaCyc:BSU22550-MON; -.
DR PRO; PR:P46912; -.
DR Proteomes; UP000001570; 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:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.20.810.10; -; 1.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00033; Cytochrome_B; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..224
FT /note="Menaquinol-cytochrome c reductase cytochrome b
FT subunit"
FT /id="PRO_0000061918"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 43
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT BINDING 94
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 108
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 196
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 211
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
SQ SEQUENCE 224 AA; 25488 MW; 871B8CEF155E8ACF CRC64;
MLNKIYDWVD ERLDITPMWR DIADHEVPEH VNPAHHFSAF VYCFGGLTFF VTVIQVLSGM
FLTMYYVPDI KNAWESVYYL QNEVAFGQIV RGMHHWGASL VIVMMFLHTL RVFFQGAYKK
PRELNWIVGV LIFFVMLGLG FTGYLLPWDM KALFATKVGL QIAEATPLIG TQVKTLLAGH
PDIVGAQTLT RFFAIHVFFL PAALFGLMAA HFIMIRKQGI SGPL
