ID A0A1S2L7F7_9BACI Unreviewed; 339 AA.
AC A0A1S2L7F7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Cytochrome d ubiquinol oxidase subunit II {ECO:0000313|EMBL:OIJ08311.1};
GN ORFNames=BKP35_17800 {ECO:0000313|EMBL:OIJ08311.1};
OS Anaerobacillus arseniciselenatis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=85682 {ECO:0000313|EMBL:OIJ08311.1, ECO:0000313|Proteomes:UP000180098};
RN [1] {ECO:0000313|EMBL:OIJ08311.1, ECO:0000313|Proteomes:UP000180098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15340 {ECO:0000313|EMBL:OIJ08311.1,
RC ECO:0000313|Proteomes:UP000180098};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-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}.
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:OIJ08311.1}.
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DR EMBL; MLQQ01000054; OIJ08311.1; -; Genomic_DNA.
DR RefSeq; WP_071314730.1; NZ_MLQQ01000054.1.
DR AlphaFoldDB; A0A1S2L7F7; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000180098; Unassembled WGS sequence.
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:UP000180098};
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..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 339 AA; 37528 MW; 825F23CA42C79886 CRC64;
MDLNVIWFIL LGVLIIGYAV LDGFDLGVGT LFYTLGKTKE EKKTLINSIG PVWDGNEVWL
LTAGGALFAA FPFVYATVFS GFYFAMLLVL FGLIFRAIAV EYYFKTEDDP HMQKLMGRLF
FIGSLLPGLL FGVAMGNVVV GIPMDEMQNY SGTFFALLNP YALLLGIVGL IGFLLQGTAY
TILKTDGELQ KRAIRLTKVF SYAIIVAWLA GTLTAQIYAP HMFTNYFNYP VLFIIPLTTV
AALIAIPMFL KMKHYGKLFV ASSLVIFTKI GTLAAGMFPN LVFSANSAPN LTIYNASSTE
LTLRVMFIIA LIGMPLVIIY TIYVYYVFRG KATPERSGY
//
