ID A0A2S2BRH7_9NOCA Unreviewed; 345 AA.
AC A0A2S2BRH7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Cytochrome d ubiquinol oxidase subunit II {ECO:0000313|EMBL:AWK71193.1};
GN ORFNames=CBI38_05965 {ECO:0000313|EMBL:AWK71193.1};
OS Rhodococcus oxybenzonivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1990687 {ECO:0000313|EMBL:AWK71193.1, ECO:0000313|Proteomes:UP000245711};
RN [1] {ECO:0000313|EMBL:AWK71193.1, ECO:0000313|Proteomes:UP000245711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2-17 {ECO:0000313|EMBL:AWK71193.1,
RC ECO:0000313|Proteomes:UP000245711};
RA Lee Y., Kim K.H., Chun B.H., Jung H.S., Jeon C.O.;
RT "Isolation of Rhodococcus sp. S2-17 biodegrading of BP-3.";
RL Submitted (MAY-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}.
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DR EMBL; CP021354; AWK71193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S2BRH7; -.
DR KEGG; roz:CBI38_05965; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000245711; 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:UP000245711};
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 79..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 200..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 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 345 AA; 37495 MW; F2B652B4CBCF7A02 CRC64;
MGLVEVWFIL IAVLFTGYFV LEGFDFGVGM LMPVLGRRKD ADGDTRRRVV LNTIGPVWDG
NEVWLITAGG ALFAAFPEWY ATLFSGFYLP LLLILVALIV RICAIEYRGK IDDDTWRRRC
DWGIVFGSWV PAVLWGVAFA NIVRGVDINA EKVVTSSLLD LLNPYALLGG LTTALLFALH
GAVFLALKTA DEVRVDAVEL AAKLALPTVP VAGAFVLWTQ LAHGKAWTWI LVAAAAAALA
GVVALTRAGR EGWAFALTSI AVIASVVLLF GSLFPDVMPS TLDAAYSLTV DNASSSPYTL
TVMTWAAAFL TPVVLLYQGW TYWVFRQRIS TKQIPPSIGL PLGRR
//
