ID D9XPX8_9ACTN Unreviewed; 334 AA.
AC D9XPX8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Cytochrome d ubiquinol oxidase, subunit II {ECO:0000313|EMBL:EFL40432.1};
GN ORFNames=SSRG_03236 {ECO:0000313|EMBL:EFL40432.1};
OS Streptomyces griseoflavus Tu4000.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL40432.1, ECO:0000313|Proteomes:UP000002968};
RN [1] {ECO:0000313|EMBL:EFL40432.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL40432.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL Submitted (FEB-2009) 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; GG657758; EFL40432.1; -; Genomic_DNA.
DR RefSeq; WP_004929314.1; NZ_GG657758.1.
DR AlphaFoldDB; D9XPX8; -.
DR STRING; 467200.SSRG_03236; -.
DR eggNOG; COG1294; Bacteria.
DR HOGENOM; CLU_049294_0_1_11; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000002968; 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 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..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..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..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 334 AA; 37085 MW; E5A3DD975B690936 CRC64;
MELHDVWFVL IAVLWIGYFF LEGFDFGVGV LTRLLARDRA EKRVLINTIG PVWDGNEVWL
LTAGGATFAA FPEWYATLFS GFYLPLLVIL VCLIVRGVAF EYRAKRPEEH WQRNWETAIF
WTSLIPAFLW GVAFGNIVRG VKIDAEFEYV GTVWDLLNPY ALLGGLVTLS LFTFHGTVFT
ALKTVGEIRA RARKLALRVG LVTAVLALVF LMWTQADRGD GTSLVAMAVA VAALVAALAA
NQAGREGWSF ALSGVTIVAA VAMLFLTLFP NVMPSTLDAD WSLTVTNASS SPYTLKIMTW
LAVIATPLVM LYQGWTYWVF RKRIGTQHIA DPVH
//
