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Database: UniProt
Entry: O66459_AQUAE
LinkDB: O66459_AQUAE
Original site: O66459_AQUAE 
ID   O66459_AQUAE            Unreviewed;       409 AA.
AC   O66459;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   SubName: Full=Cytochrome b {ECO:0000313|EMBL:AAC06424.1};
GN   Name=petB {ECO:0000313|EMBL:AAC06424.1};
GN   OrderedLocusNames=aq_044 {ECO:0000313|EMBL:AAC06424.1};
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324 {ECO:0000313|EMBL:AAC06424.1, ECO:0000313|Proteomes:UP000000798};
RN   [1] {ECO:0000313|EMBL:AAC06424.1, ECO:0000313|Proteomes:UP000000798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5 {ECO:0000313|EMBL:AAC06424.1,
RC   ECO:0000313|Proteomes:UP000000798};
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olson G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
RN   [2] {ECO:0007829|PDB:6KLS, ECO:0007829|PDB:6KLV}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS).
RX   PubMed=31778296; DOI=10.1002/anie.201911554;
RA   Zhu G., Zeng H., Zhang S., Juli J., Pang X., Hoffmann J., Zhang Y.,
RA   Morgner N., Zhu Y., Peng G., Michel H., Sun F.;
RT   "A 3.3A-Resolution Structure of Hyperthermophilic Respiratory ComplexIII
RT   Reveals the Mechanism of Its Thermal Stability.";
RL   Angew. Chem. Int. Ed. 59:343-351(2020).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; AE000657; AAC06424.1; -; Genomic_DNA.
DR   PIR; H70303; H70303.
DR   RefSeq; NP_213019.1; NC_000918.1.
DR   RefSeq; WP_010879957.1; NC_000918.1.
DR   PDB; 6KLS; EM; 3.30 A; B/E=1-409.
DR   PDB; 6KLV; EM; 3.20 A; B/E=1-409.
DR   AlphaFoldDB; O66459; -.
DR   EMDB; EMD-0716; -.
DR   EMDB; EMD-0719; -.
DR   SMR; O66459; -.
DR   STRING; 224324.aq_044; -.
DR   EnsemblBacteria; AAC06424; AAC06424; aq_044.
DR   KEGG; aae:aq_044; -.
DR   PATRIC; fig|224324.8.peg.35; -.
DR   eggNOG; COG1290; Bacteria.
DR   HOGENOM; CLU_031114_3_0_0; -.
DR   InParanoid; O66459; -.
DR   OrthoDB; 9804503at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; PF13631; Cytochrom_B_N_2; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:6KLS, ECO:0007829|PDB:6KLV};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Heme {ECO:0000256|ARBA:ARBA00022617}; 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:UP000000798};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        38..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        94..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        257..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          7..229
FT                   /note="Cytochrome b/b6 N-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51002"
FT   DOMAIN          235..404
FT                   /note="Cytochrome b/b6 C-terminal region profile"
FT                   /evidence="ECO:0000259|PROSITE:PS51003"
SQ   SEQUENCE   409 AA;  46928 MW;  E524BE04CC06607A CRC64;
     MGLIEKIVDW IDERAHVREI YRTQMVEYKV AKNLTFPYVF GILALVTFAI QIISGMVLIL
     YYNLQSQTLL TVHLLDNGRN SLRMALQAHT RTGANFFMAI VYLHMFTGIY YNAYKRPREL
     VWIVGWLIYF VLILTALSGY LLPWGQLSYW GFIVTTEIPG SLADAPILKP IFKAIAETIV
     LWMKGGYVVT DVTLGRVFGS HVLIYPLILL ALVGIHLYLV RAAGISNPEG IEYDKKKNPD
     KFVPFHPYMT LKEGAYVMWY LAVFFFFVFF HISHFLPPEN FEPANPLKTP AHIAPEWYLL
     GYYEVFRSIP SKFWGFVAFN ALLLLLLLLP FLDFSPLKSA RRRPLFFVMF VIFMISSMAL
     TILGTMPPTP QNAKLGLIFA ALVFAFFISL PIISFIEYGW YKAKGGQQE
//
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