ID   A0A239CFP3_9ACTN        Unreviewed;       313 AA.
AC   A0A239CFP3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Cytochrome bd-I ubiquinol oxidase subunit 2 apoprotein {ECO:0000313|EMBL:SNS18498.1};
GN   ORFNames=SAMN05216276_1005160 {ECO:0000313|EMBL:SNS18498.1};
OS   Streptosporangium subroseum.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=106412 {ECO:0000313|EMBL:SNS18498.1, ECO:0000313|Proteomes:UP000198282};
RN   [1] {ECO:0000313|EMBL:SNS18498.1, ECO:0000313|Proteomes:UP000198282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNS18498.1,
RC   ECO:0000313|Proteomes:UP000198282};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-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; FZOD01000005; SNS18498.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239CFP3; -.
DR   OrthoDB; 9776710at2; -.
DR   Proteomes; UP000198282; 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:UP000198282};
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..35
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..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        144..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        178..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   313 AA;  32747 MW;  6E84AE0AD5E7B6E2 CRC64;
     MELTTFWFAV IAFLWTGYFV LEGFDFGVGM LAPVLSRNEA ERKQVLGTIG PVWDGNEVWL
     ITAVGAMFAA FPAWYAGLLS TFYLPIALVL VGLIVRGIGL EWRGKVHSST GRARADLGIL
     IGSFLPAFLW GAIFADLLHG SATAALAGGI FSLSLCVLHG AVFVALKTSG PVRSRARRTA
     MITSAVALPA AVVALSGIPG ASASVSDWAA APWLWACALA AMAALSAGIA LTWRGRDGWA
     FAATASSIAG TGAALFGALS PAPLPGLTIA EAASGPYTLN VLTWIGLVAL PFVLGYQAWS
     YWVFRKRLVA EVS
//