ID A0A1Q9LM51_9PSEU Unreviewed; 335 AA.
AC A0A1Q9LM51;
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:OLR93116.1};
GN ORFNames=BJP25_00485 {ECO:0000313|EMBL:OLR93116.1};
OS Actinokineospora bangkokensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=1193682 {ECO:0000313|EMBL:OLR93116.1, ECO:0000313|Proteomes:UP000186040};
RN [1] {ECO:0000313|EMBL:OLR93116.1, ECO:0000313|Proteomes:UP000186040}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=44EHW {ECO:0000313|EMBL:OLR93116.1,
RC ECO:0000313|Proteomes:UP000186040};
RA Greule A., Intra B., Flemming S., Rommel M.G., Panbangred W., Bechthold A.;
RT "The Draft Genome Sequence of Actinokineospora bangkokensis 44EHWT reveals
RT the biosynthetic pathway of antifungal compounds Thailandins with unusual
RT extender unit butylmalonyl-CoA.";
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:OLR93116.1}.
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DR EMBL; MKQR01000012; OLR93116.1; -; Genomic_DNA.
DR RefSeq; WP_075975112.1; NZ_MKQR01000012.1.
DR AlphaFoldDB; A0A1Q9LM51; -.
DR STRING; 1193682.BJP25_00485; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000186040; 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:UP000186040};
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..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..183
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 335 AA; 35627 MW; ECD223D56C757D68 CRC64;
MELSIVWFCV IALLWLGYLF LEGFDFGVGM LMPFLAKDNT ERRVMVNTIG PVWDGNEVWV
IVAIGATFAA FPGWYASLLS AAYLPVLCVL LGLIGRGVAF EYRGKVDSDR WRAAWDKVIF
TGSLVPALGI GLLIATTVFG LPLDAEGNRV GPVLAAVRPE TLLGAAAVVG FALVHGAVFT
SLKTDGDIRH RARELALRLG PLALVPLGAL VVLAQLRSGS GWTWLAAGVA GAAALVSFAR
LLRGREGQAF AALGVVIAAS VVALFGSLYP NVLPSTLDPA WSLTVEGAAS SPYALGVMSW
VALFGTPAVL IYQAWTYWVF RKRVSTAHIP PVHVP
//
