ID A0A160FB50_9BACI Unreviewed; 336 AA.
AC A0A160FB50;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Cytochrome d ubiquinol oxidase, subunit II {ECO:0000313|EMBL:ANB63871.1};
GN Name=cydB {ECO:0000313|EMBL:ANB63871.1};
GN ORFNames=GFC29_2465 {ECO:0000313|EMBL:ANB63871.1};
OS Anoxybacillus sp. B7M1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1490057 {ECO:0000313|EMBL:ANB63871.1, ECO:0000313|Proteomes:UP000076753};
RN [1] {ECO:0000313|EMBL:ANB63871.1, ECO:0000313|Proteomes:UP000076753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=b7m1 {ECO:0000313|Proteomes:UP000076753};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; CP015436; ANB63871.1; -; Genomic_DNA.
DR RefSeq; WP_044742375.1; NZ_CP015436.1.
DR AlphaFoldDB; A0A160FB50; -.
DR KEGG; anl:GFC29_2465; -.
DR PATRIC; fig|1490057.3.peg.2783; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000076753; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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 Reference proteome {ECO:0000313|Proteomes:UP000076753};
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 6..36
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..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 336 AA; 37508 MW; 6C9A3586F56B50BA CRC64;
MALNELWFIL VAVLFIGFFF LEGFDFGVGM AGRFLGKNDV ERRIMINTIG PFWDANEVWL
LTGGGAIFAA FPHWYATMFS GYYIPFVFVL LALIGRGVAF EFRGKVDHPS WKQTWDWIIF
FGSILPPFLF GVLFSSILRG MPIDQSMTLH AEFSDYVNIY TVTGGVAVTL LCFLHGLLFL
TLKTVGDLQM RARKLAQKMI YAVLAALVVF VGLSYTETDL FTYRGEVTVP LVALVVVSYG
LVILFSKKGR DGWTFAMSGL GIALTVGAIF AGLFPRVMIS SISSAYDLTI YNAASGAYSL
KVMTIVAVTL LPFVLGYQIW SYYVFRKRVD GKDMVY
//
