ID K0NFL8_DESTT Unreviewed; 342 AA.
AC K0NFL8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=CydB: cytochrome d ubiquinol oxidase, subunit II {ECO:0000313|EMBL:CCK79921.1};
DE EC=1.10.3.- {ECO:0000313|EMBL:CCK79921.1};
GN Name=cydB {ECO:0000313|EMBL:CCK79921.1};
GN OrderedLocusNames=TOL2_C17600 {ECO:0000313|EMBL:CCK79921.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK79921.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK79921.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 2
CC family. {ECO:0000256|ARBA:ARBA00007543}.
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DR EMBL; FO203503; CCK79921.1; -; Genomic_DNA.
DR RefSeq; WP_014957262.1; NC_018645.1.
DR AlphaFoldDB; K0NFL8; -.
DR STRING; 651182.TOL2_C17600; -.
DR KEGG; dto:TOL2_C17600; -.
DR PATRIC; fig|651182.5.peg.2099; -.
DR HOGENOM; CLU_049294_0_1_7; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR003317; Cyt-d_oxidase_su2.
DR NCBIfam; TIGR00203; cydB; 1.
DR PANTHER; PTHR43141:SF5; CYTOCHROME BD-I UBIQUINOL OXIDASE SUBUNIT 2; 1.
DR PANTHER; PTHR43141; CYTOCHROME BD2 SUBUNIT II; 1.
DR Pfam; PF02322; Cyt_bd_oxida_II; 1.
DR PIRSF; PIRSF000267; Cyt_oxidse_sub2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 Oxidoreductase {ECO:0000313|EMBL:CCK79921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
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 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 300..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 342 AA; 38706 MW; 1AEB3C26B0BAC3AF CRC64;
MLLQYTWFYL WGLLWAVFFM TDGFDFGIGT LYPFLGKSDR DKRVMINSIG PLWDGNEVWL
ITAGGVTFAA FPQVYATMFS SLYTPLMLIL FALIFRGVAF EFRGKIESNG WKKLWDTFIF
LGSFLPALLF GVAFANIFQG IPFDGDGIYH GNTLKLLNPY GLLGGVLFVL LFLQHGANWL
NIKTTGELRE RSILVSKKIW LFLVPVAVIF LIASYFTTSL YENYFKTPAM FLVILATVAA
LFATRFFIEK QLFFKAWFAS ALTIVGAIFF GVIGLFPALF PSSMDKAFSL TAFNASSSPL
TLKIMLGVVL VFIPIVIIYQ AWAYHFFKEP VTQEDLDMDE AY
//