CYB_RHOCB
ID CYB_RHOCB Reviewed; 437 AA.
AC D5ANZ3; P07057; P08502;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Cytochrome b;
GN Name=petB; Synonyms=cytB; OrderedLocusNames=RCAP_rcc02769;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=2821268; DOI=10.1016/0022-2836(87)90323-8;
RA Davidson E., Daldal F.;
RT "Primary structure of the bc1 complex of Rhodopseudomonas capsulata.
RT Nucleotide sequence of the pet operon encoding the Rieske cytochrome b, and
RT cytochrome c1 apoproteins.";
RL J. Mol. Biol. 195:13-24(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
RN [3]
RP MUTAGENESIS OF PHE-144.
RC STRAIN=MT1131;
RX PubMed=2176897; DOI=10.1021/bi00503a014;
RA Robertson D.E., Daldal F., Dutton P.L.;
RT "Mutants of ubiquinol-cytochrome c2 oxidoreductase resistant to Qo site
RT inhibitors: consequences for ubiquinone and ubiquinol affinity and
RT catalysis.";
RL Biochemistry 29:11249-11260(1990).
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 {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC Note=Binds 2 heme b groups non-covalently. {ECO:0000250};
CC -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC cytochrome c1 and the Rieske protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- MISCELLANEOUS: Heme 1 (or BL or b562) is low-potential and absorbs at
CC about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs
CC at about 566 nm. {ECO:0000250}.
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; X05630; CAA29117.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE86498.1; -; Genomic_DNA.
DR PIR; B29336; B29336.
DR RefSeq; WP_013068476.1; NC_014034.1.
DR PDB; 6XI0; EM; 3.30 A; C/P=1-437.
DR PDB; 6XKT; EM; 3.75 A; C/P=1-437.
DR PDB; 6XKU; EM; 4.20 A; C/P=1-437.
DR PDB; 6XKV; EM; 3.50 A; C/P=1-437.
DR PDB; 6XKW; EM; 5.20 A; C/P=1-437.
DR PDB; 6XKX; EM; 6.10 A; C/P=1-437.
DR PDB; 6XKZ; EM; 7.20 A; C/P=1-437.
DR PDBsum; 6XI0; -.
DR PDBsum; 6XKT; -.
DR PDBsum; 6XKU; -.
DR PDBsum; 6XKV; -.
DR PDBsum; 6XKW; -.
DR PDBsum; 6XKX; -.
DR PDBsum; 6XKZ; -.
DR AlphaFoldDB; D5ANZ3; -.
DR SMR; D5ANZ3; -.
DR STRING; 272942.RCAP_rcc02769; -.
DR EnsemblBacteria; ADE86498; ADE86498; RCAP_rcc02769.
DR GeneID; 31491587; -.
DR KEGG; rcp:RCAP_rcc02769; -.
DR eggNOG; COG1290; Bacteria.
DR HOGENOM; CLU_031114_3_0_5; -.
DR OMA; RFFAFHF; -.
DR OrthoDB; 262439at2; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045275; C:respiratory chain complex III; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
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; 1.20.810.10; -; 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; IPR027387; Cytb/b6-like_sf.
DR InterPro; IPR030689; Cytochrome_b.
DR InterPro; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 1.
DR PIRSF; PIRSF038885; COB; 1.
DR SUPFAM; SSF81342; SSF81342; 1.
DR SUPFAM; SSF81648; SSF81648; 1.
DR PROSITE; PS51003; CYTB_CTER; 1.
DR PROSITE; PS51002; CYTB_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Electron transport; Heme; Iron; Membrane;
KW Metal-binding; Reference proteome; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..437
FT /note="Cytochrome b"
FT /id="PRO_0000409864"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 97
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 111
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 198
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 212
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 MUTAGEN 144
FT /note="F->L,S: Loss of binding affinity for ubiquinone and
FT ubiquinol."
FT /evidence="ECO:0000269|PubMed:2176897"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 47..65
FT /evidence="ECO:0007829|PDB:6XI0"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:6XI0"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 91..117
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 126..147
FT /evidence="ECO:0007829|PDB:6XI0"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 154..168
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 173..181
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6XI0"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 247..269
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:6XI0"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 317..320
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 328..345
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 361..380
FT /evidence="ECO:0007829|PDB:6XI0"
FT HELIX 389..414
FT /evidence="ECO:0007829|PDB:6XI0"
SQ SEQUENCE 437 AA; 49350 MW; F1A21D35DCE8C7A8 CRC64;
MSGIPHDHYE PKTGIEKWLH DRLPIVGLVY DTIMIPTPKN LNWWWIWGIV LAFTLVLQIV
TGIVLAMHYT PHVDLAFASV EHIMRDVNGG WAMRYIHANG ASLFFLAVYI HIFRGLYYGS
YKAPREITWI VGMVIYLLMM GTAFMGYVLP WGQMSFWGAT VITGLFGAIP GIGPSIQAWL
LGGPAVDNAT LNRFFSLHYL LPFVIAALVA IHIWAFHTTG NNNPTGVEVR RTSKADAEKD
TLPFWPYFVI KDLFALALVL LGFFAVVAYM PNYLGHPDNY VQANPLSTPA HIVPEWYFLP
FYAILRAFAA DVWVVILVDG LTFGIVDAKF FGVIAMFGAI AVMALAPWLD TSKVRSGAYR
PKFRMWFWFL VLDFVVLTWV GAMPTEYPYD WISLIASTYW FAYFLVILPL LGATEKPEPI
PASIEEDFNS HYGNPAE
