CYBC_BRADU
ID CYBC_BRADU Reviewed; 687 AA.
AC P51131;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cytochrome b/c1;
DE Contains:
DE RecName: Full=Cytochrome b;
DE Contains:
DE RecName: Full=Cytochrome c1;
GN Name=fbcH; OrderedLocusNames=blr2486;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MEMBRANE LOCALIZATION, AND PROTEOLYTIC
RP PROCESSING.
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110, and
RC USDA 110RIF15;
RX PubMed=2541921; DOI=10.1016/0092-8674(89)90137-2;
RA Thoeny-Meyer L., Stax D., Hennecke H.;
RT "An unusual gene cluster for the cytochrome bc1 complex in Bradyrhizobium
RT japonicum and its requirement for effective root nodule symbiosis.";
RL Cell 57:683-697(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [3]
RP PROTEIN SEQUENCE OF 435-444, AND MUTAGENESIS OF THE INTERNAL SIGNAL
RP SEQUENCE AND OF THE CYTOCHROME C1 HEME-BINDING RESIDUES.
RC STRAIN=USDA 110spc4;
RX PubMed=1647023; DOI=10.1073/pnas.88.11.5001;
RA Thoeny-Meyer L., James P., Hennecke H.;
RT "From one gene to two proteins: the biogenesis of cytochromes b and c1 in
RT Bradyrhizobium japonicum.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:5001-5005(1991).
CC -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase complex
CC (complex III or cytochrome b-c1 complex), which is a respiratory chain
CC that generates an electrochemical potential coupled to ATP synthesis.
CC c1 functions as an electron donor to cytochrome c.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Note=Binds 2 heme b groups non-covalently. Heme 1 (or bL or b562) is
CC low-potential and absorbs at about 562 nm, and heme 2 (or bH or b566)
CC is high-potential and absorbs at about 566 nm.;
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Note=Binds 1 heme c group covalently. Heme 3 is covalently bound to
CC cytochrome c1.;
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Required for nitrogen fixation in root nodules on
CC soybeans, but not for aerobic growth. It seems to be expressed under
CC many growth conditions (aerobic, microaerobic and in nodule
CC bacteroids).
CC -!- PTM: The protein is post-translationally processed into cytochrome b
CC and c1. This occurs by processing between residues 434 and 435 without
CC processing between cytochrome b and the N-terminal of the putative
CC signal sequence domain. {ECO:0000269|PubMed:2541921}.
CC -!- SIMILARITY: Belongs to the cytochrome b family. {ECO:0000255|PROSITE-
CC ProRule:PRU00967, ECO:0000255|PROSITE-ProRule:PRU00968}.
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DR EMBL; J03176; AAA26200.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC47751.1; -; Genomic_DNA.
DR PIR; B32382; B32382.
DR RefSeq; NP_769126.1; NC_004463.1.
DR RefSeq; WP_011085273.1; NZ_CP011360.1.
DR AlphaFoldDB; P51131; -.
DR SMR; P51131; -.
DR STRING; 224911.27350742; -.
DR EnsemblBacteria; BAC47751; BAC47751; BAC47751.
DR GeneID; 64022228; -.
DR KEGG; bja:blr2486; -.
DR PATRIC; fig|224911.44.peg.2057; -.
DR eggNOG; COG1290; Bacteria.
DR eggNOG; COG2857; Bacteria.
DR HOGENOM; CLU_021957_1_0_5; -.
DR InParanoid; P51131; -.
DR OMA; LPWLDSA; -.
DR PhylomeDB; P51131; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProt.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; 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 CDD; cd00290; cytochrome_b_C; 1.
DR CDD; cd00284; Cytochrome_b_N; 1.
DR Gene3D; 1.10.760.10; -; 1.
DR Gene3D; 1.20.810.10; -; 1.
DR InterPro; IPR005798; Cyt_b/b6_C.
DR InterPro; IPR036150; Cyt_b/b6_C_sf.
DR InterPro; IPR005797; Cyt_b/b6_N.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR002326; Cyt_c1.
DR InterPro; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF02167; Cytochrom_C1; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR PRINTS; PR00603; CYTOCHROMEC1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
DR PROSITE; PS51007; CYTC; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Electron transport; Heme; Iron; Membrane; Metal-binding;
KW Reference proteome; Respiratory chain; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..434
FT /note="Cytochrome b"
FT /id="PRO_0000006468"
FT CHAIN 435..687
FT /note="Cytochrome c1"
FT /id="PRO_0000006469"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 666..678
FT /note="Helical; Note=Anchors to the membrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00967,
FT ECO:0000255|PROSITE-ProRule:PRU00968"
FT DOMAIN 458..643
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 404..434
FT /note="Internal signal sequence"
FT BINDING 96
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 110
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 197
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b562"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 211
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_label="b566"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 471
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 474
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT BINDING 475
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 616
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT MUTAGEN 432..434
FT /note="Missing: Individual cytochrome b and c1 are not
FT detected, instead a larger protein which is probably the
FT FbcH precursor protein is detected. Cytochrome c oxidase
FT activity is not affected."
FT /evidence="ECO:0000269|PubMed:1647023"
FT MUTAGEN 432
FT /note="A->D: Individual cytochrome b and c1 are not
FT detected, instead a larger protein which is probably the
FT FbcH precursor protein is detected. Cytochrome c oxidase
FT activity is not affected."
FT /evidence="ECO:0000269|PubMed:1647023"
FT MUTAGEN 471..474
FT /note="CASC->SASS: No cytochrome c oxidase activity, no
FT cytochrome b, c1 or precursor protein detected."
FT /evidence="ECO:0000269|PubMed:1647023"
SQ SEQUENCE 687 AA; 76470 MW; A58048F1CF1EFFBB CRC64;
MSGPSDYQPS NPALQWIERR LPILGLMHSS FVAYPTPRNL NYWWTFGAIL SFMLGMQILT
GVILAMHYTP HADLAFKSVE LIVRDVNYGW LLRNMHACGA SMFFFAVYVH MLRGLYYGSY
KEPREVLWIL GVIIYLLMMA TGFMGYVLPW GQMSFWGATV ITNLFSAIPY FGESIVTLLW
GGYSVGNPTL NRFFSLHYLL PFLIAGVVVL HVWALHVAGQ NNPEGVEPKS EKDTVPFTPH
ATIKDMFGVA CFLLLYAWFI FYMPNYLGDA DNYIPANPGV TPPHIVPEWY YLPFYAILRS
IPNKLAGVIG MFSAIIILCF LPWLDAAKTR SSKYRPLAKQ FFWIFVAVCI LLGYLGAQPP
EGIYVIAGRV LTVCYFAYFL IVLPLLSRIE TPRPVPNSIS EAILAKGGKA VASVAIALVA
AGALFLGSLQ DARANEGSDK PPGNKWSFAG PFGKFDRGAL QRGLKVYKEV CASCHGLSYI
AFRNLAEAGG PSYSVAQVAA FASDYKIKDG PNDAGDMFER PGRPADYFPS PFPNEQAARA
ANGGAAPPDL SLITKARSYG RGFPWFIFDF FTQYQEQGPD YVSAVLQGFE EKVPEGVTIP
EGSYYNKYFP GHAIKMPKPL SDGQVTYDDG SPATVAQYSK DVTTFLMWTA EPHMEARKRL
GFQVFVFLII FAGLMYFTKK KVWADSH
