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Database: UniProt
Entry: A0A1P8UF97_9GAMM
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Original site: A0A1P8UF97_9GAMM 
ID   A0A1P8UF97_9GAMM        Unreviewed;       429 AA.
AC   A0A1P8UF97;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Cytochrome b {ECO:0000256|RuleBase:RU003385};
GN   ORFNames=BW247_04475 {ECO:0000313|EMBL:APZ42434.1};
OS   Acidihalobacter ferrooxydans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=1765967 {ECO:0000313|EMBL:APZ42434.1, ECO:0000313|Proteomes:UP000243807};
RN   [1] {ECO:0000313|EMBL:APZ42434.1, ECO:0000313|Proteomes:UP000243807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V8 {ECO:0000313|EMBL:APZ42434.1,
RC   ECO:0000313|Proteomes:UP000243807};
RA   Khaleque H.N., Ramsay J.P., Murphy R.J.T., Kaksonen A.H., Boxall N.J.,
RA   Watkin E.L.J.;
RT   "Draft sequence of Acidihalobacter ferrooxidans strain DSM 14175 (strain
RT   V8).";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU003385}.
CC   -!- COFACTOR:
CC       Name=heme b; Xref=ChEBI:CHEBI:60344;
CC         Evidence={ECO:0000256|RuleBase:RU003385};
CC       Note=Binds 2 heme groups non-covalently.
CC       {ECO:0000256|RuleBase:RU003385};
CC   -!- SUBUNIT: The main subunits of complex b-c1 are: cytochrome b,
CC       cytochrome c1 and the Rieske protein. {ECO:0000256|ARBA:ARBA00011649,
CC       ECO:0000256|RuleBase:RU003385}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the cytochrome b family.
CC       {ECO:0000256|RuleBase:RU003385}.
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DR   EMBL; CP019434; APZ42434.1; -; Genomic_DNA.
DR   RefSeq; WP_076836038.1; NZ_CP019434.1.
DR   AlphaFoldDB; A0A1P8UF97; -.
DR   STRING; 1765967.BW247_04475; -.
DR   OrthoDB; 9804503at2; -.
DR   Proteomes; UP000243807; Chromosome.
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   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   PANTHER; PTHR19271; CYTOCHROME B; 1.
DR   PANTHER; PTHR19271:SF16; CYTOCHROME B; 1.
DR   Pfam; PF00032; Cytochrom_B_C; 1.
DR   Pfam; PF00033; Cytochrome_B; 1.
DR   SUPFAM; SSF81648; a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase); 1.
DR   SUPFAM; SSF81342; Transmembrane di-heme cytochromes; 1.
DR   PROSITE; PS51003; CYTB_CTER; 1.
DR   PROSITE; PS51002; CYTB_NTER; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|RuleBase:RU003385};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU003385};
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243807};
KW   Respiratory chain {ECO:0000256|RuleBase:RU003385};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003385};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003385}.
FT   TRANSMEM        32..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        183..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        307..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        336..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..213
FT                   /note="Cytochrome b/b6 N-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51002"
FT   DOMAIN          223..396
FT                   /note="Cytochrome b/b6 C-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51003"
SQ   SEQUENCE   429 AA;  48570 MW;  1AEEC5CFB6E7B1F8 CRC64;
     MANALEWFYR RVPMDLYREH LSEYPAPKNF NIGYYMGSLL LVMVALQFVT GLLLMMQYNP
     AQPVQSIQNI TQHVWYGWLI WLMHTDGVSF FFALLYLHMA RGLMYGSYKT PRELVWVAGW
     FIFLLSAGEA FIGYTLPGMA TSYAASDVIS QLLAGGAWYG NWAFQLVLGG RSYGAPMLMR
     FEAFHVVLLF TLLVVMIVVH VLLLHRVGSN NPDGVDTHSR TNAKGWPLDG IPFHPYFTVK
     DMVGIGVFFL IFAAVLLYNP SMNGWFISSG DVQPANPLYF GGIDIRAPWY LSPFYQLLRA
     SPSNNQGQMI FWVGLLMPFF LPWLDRNPVR SIRYRPIYAV WLFLLFADMI GMMIVGSEPA
     MPYTLFPERI LTVFYFAWFM LLPMVSGIEV MLMHPPHVPA RVGDGLMGRI MHGGALRARG
     QGGSNGGES
//
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