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Entry: A0A2A2F5K5_9GAMM
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ID   A0A2A2F5K5_9GAMM        Unreviewed;       411 AA.
AC   A0A2A2F5K5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Cytochrome b {ECO:0000256|ARBA:ARBA00013531, ECO:0000256|RuleBase:RU003385};
GN   ORFNames=CK501_12220 {ECO:0000313|EMBL:PAU79957.1};
OS   Halovibrio salipaludis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halovibrio.
OX   NCBI_TaxID=2032626 {ECO:0000313|EMBL:PAU79957.1, ECO:0000313|Proteomes:UP000218896};
RN   [1] {ECO:0000313|EMBL:PAU79957.1, ECO:0000313|Proteomes:UP000218896}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YL5-2 {ECO:0000313|EMBL:PAU79957.1,
RC   ECO:0000313|Proteomes:UP000218896};
RA   Dong X., Zhang G.;
RT   "Halovibrio sewagensis sp. nov., isolated from wastewater of high
RT   salinity.";
RL   Submitted (AUG-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|ARBA:ARBA00002444, 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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038885-2};
CC       Note=Binds 2 heme groups non-covalently.
CC       {ECO:0000256|PIRSR:PIRSR038885-2};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAU79957.1}.
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DR   EMBL; NSKD01000005; PAU79957.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2F5K5; -.
DR   OrthoDB; 9804503at2; -.
DR   Proteomes; UP000218896; Unassembled WGS sequence.
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; cd00284; Cytochrome_b_N; 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; IPR048259; Cytochrome_b_N_euk/bac.
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   PIRSF; PIRSF038885; COB; 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|PIRSR:PIRSR038885-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038885-2};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038885-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218896};
KW   Respiratory chain {ECO:0000256|ARBA:ARBA00022660,
KW   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        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        118..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        145..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        184..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        314..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        346..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        377..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..216
FT                   /note="Cytochrome b/b6 N-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51002"
FT   DOMAIN          226..406
FT                   /note="Cytochrome b/b6 C-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51003"
FT   BINDING         87
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:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         101
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:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         188
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:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         203
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:0000256|PIRSR:PIRSR038885-2"
FT   BINDING         208
FT                   /ligand="a ubiquinone"
FT                   /ligand_id="ChEBI:CHEBI:16389"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038885-1"
SQ   SEQUENCE   411 AA;  46877 MW;  A6A187E713044A63 CRC64;
     MNKLIQWVDE RLPVVDAFER HMSKYYAPKN FNVWYVFGVL SMLVLVNQLL TGIWLTMMYT
     PTAEGAFASV EYIMRDVEYG WLLRYMHSTG ASMFFLVVYL HMFRGLMYGS YQKPRELIWI
     FGMAIYLILM AEAFMGYVLP WGQMSYWGAQ VIINLFSAIP GIGEDLALWI RGDYLISGAT
     LNRFFALHVV ALPIVLLGLV VLHILALHEV GSNNPDGIDI KKNKDADGKP KDGIPFHPYY
     TVHDLVPIAV FLAVFAIVVF YFPEMGGYFI EKPNFQEADP LQTPDHIAPV WYFTPFYAML
     RAITFNLFGL SSQFWGVIVM GAAIAILFVL PWLDRSPVRS MRYKGWFSRG ALALFAVSFV
     MLGYLGAEPA TPIKTMLAQI GTAIYFGYFI LMPFYTRMES TKPVPERVTT K
//
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