ID A0A1N6L4S7_9BURK Unreviewed; 378 AA.
AC A0A1N6L4S7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Cytochrome bd-I ubiquinol oxidase subunit 2 apoprotein {ECO:0000313|EMBL:SIO63784.1};
GN ORFNames=SAMN05444165_5983 {ECO:0000313|EMBL:SIO63784.1};
OS Paraburkholderia phenazinium.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=60549 {ECO:0000313|EMBL:SIO63784.1, ECO:0000313|Proteomes:UP000185151};
RN [1] {ECO:0000313|EMBL:SIO63784.1, ECO:0000313|Proteomes:UP000185151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS95 {ECO:0000313|EMBL:SIO63784.1,
RC ECO:0000313|Proteomes:UP000185151};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FSRU01000002; SIO63784.1; -; Genomic_DNA.
DR RefSeq; WP_074300881.1; NZ_FSRU01000002.1.
DR AlphaFoldDB; A0A1N6L4S7; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000185151; 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:UP000185151};
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..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 378 AA; 41199 MW; 0FB2691BDCEDEE5F CRC64;
MDYATLKVIW WVLIGVLLIG FALTDGFDMG TAILLPFIAK TDTERRIVVN TVGATWEGNQ
VWFITAGGAM FAAWPLVYAA SFSGFYFAML LVLFSLFFRP VGFDYRSKRE DPRWRSAWDW
ALFIGGFVPA LVIGVAFGNL LQGVPFSFDT DLRVTYHGSF FALLNPFAVL CGLVSVSMLA
AHGAAFVKMK TDDVIARRAS LALRIASLAG VVLFLVAGAL VATMIGGYQI VDAAPFDTVA
NPLLKSVIGA PGLWLTNYST YPWMVAAPVI GVVGGMLAVL LASSRFEKSA FICTGLMIVG
VILTAGFSMF PFIMPSSLDG RSSLTVWDST SSQMTLQIML IAVIIFLPII LIYTSWVYRV
MRGKVTRAAL EENSHSMY
//
