ID A0A2A9D2F2_9MICO Unreviewed; 345 AA.
AC A0A2A9D2F2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cytochrome bd-I ubiquinol oxidase subunit 2 apoprotein {ECO:0000313|EMBL:PFG20122.1};
GN ORFNames=ATL40_1707 {ECO:0000313|EMBL:PFG20122.1};
OS Serinibacter salmoneus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Serinibacter.
OX NCBI_TaxID=556530 {ECO:0000313|EMBL:PFG20122.1, ECO:0000313|Proteomes:UP000224915};
RN [1] {ECO:0000313|EMBL:PFG20122.1, ECO:0000313|Proteomes:UP000224915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21801 {ECO:0000313|EMBL:PFG20122.1,
RC ECO:0000313|Proteomes:UP000224915};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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:PFG20122.1}.
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DR EMBL; PDJD01000001; PFG20122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9D2F2; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000224915; 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:UP000224915};
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..28
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..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..273
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 345 AA; 37760 MW; 92C20D82102E7B43 CRC64;
MDLALLWFIL IAVLWTGYLV LEGFDFGVGM LMKPLAKDDT DRRVAINTIA PVWDGNEVWL
LTAGGATFAA FPHWYATMFS GFYLPLLLIL LALIVRGVSF EYRHKGSTQA WRNGWDWCIA
IGSWVPAILW GVAFANLVRG LEIDSEMQYV GGFWALLSPF ALLGGLVTLG LFLTHGAVFL
ALKTSGDYQT RAADLAIKLA LPSAAVAAVW VIWAQLAYSR NAWTWAPLVI AALALVGVVL
TTRARREGWA FTLNAVAIAM AVVFIFGSIY PNVMPANDPA NSLTIANSSS SDYTLMVMTW
VAVFLVPLVL LYQGWSFHVF RKRLSRESIP SSPPPAAESE SVGAH
//
