CYB6_CHLTI
ID CYB6_CHLTI Reviewed; 428 AA.
AC Q59297;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Cytochrome bc complex cytochrome b subunit;
GN Name=petB;
OS Chlorobaculum thiosulfatiphilum (Chlorobium limicola f.sp.
OS thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=115852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-25.
RA Schuetz M., Zirngibl S., le Coutre J., Buettner M., Xie D.-L., Nelson N.,
RA Deutzmann R., Hauska G.;
RT "A transcription unit for the Rieske FeS-protein and cytochrome b in
RT Chlorobium limicola.";
RL Photosyn. Res. 39:163-174(1994).
CC -!- FUNCTION: Component of the green S-bacteria bc complex, which consists
CC of the Rieske protein and cytochrome b subunit but appears to lack a
CC cytochrome c1-equivalent. This complex has a comparatively low redox
CC potential.
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 -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane 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; X73628; CAA52008.1; -; Genomic_DNA.
DR PIR; S38461; S38461.
DR AlphaFoldDB; Q59297; -.
DR SMR; Q59297; -.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
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; 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; IPR016174; Di-haem_cyt_TM.
DR Pfam; PF00032; Cytochrom_B_C; 1.
DR Pfam; PF00033; Cytochrome_B; 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 Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Electron transport; Heme; Iron; Membrane; Metal-binding; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.1"
FT CHAIN 2..428
FT /note="Cytochrome bc complex cytochrome b subunit"
FT /id="PRO_0000061916"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 175
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 261
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
FT BINDING 276
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00968"
SQ SEQUENCE 428 AA; 47477 MW; 83F6EFF0894515A2 CRC64;
MAENTPKPAA GTAPAKPKPA APGAAKPAAP KAARPGAAKP AAKPAAPRAA APSGVYKKPP
VDRPDPNPFK DSKRDAVAGW FQERFYVLNP IIDYLKHKEV PKHALSFWYY FGGLGLFFFV
IQILTGLLLL QYYKPTETDA FASFLFIQGE VPFGWLLRQI HAWSANLMIM MLFIHMFSTF
FMKSYRKPRE LMWVSGFVLL LLSLGFGFTG YLLPWNELAF FATQVGTEVP KVAPGGAFLV
EILRGGPEVG GETLTRMFSL HVVLLPGLVM LVLAAHLTLV QILGTSAPIG YKEAGLIKGY
DKFFPTFLAK DGIGWLIGFA LLIYLAVMFP WEIGVKANPL SPAPLGIKPE WYFWAQFQLL
KDFKFEGGEL LAIILFTIGG VVWLLVPFID RQASEEKKSP IFTIFGILVL AFLLINTYRV
YAEYSMLK
