ID A0A1D9MDL6_9RHOB Unreviewed; 387 AA.
AC A0A1D9MDL6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cytochrome d ubiquinol oxidase subunit II {ECO:0000313|EMBL:AOZ69946.1};
GN ORFNames=LPB142_11930 {ECO:0000313|EMBL:AOZ69946.1};
OS Rhodobacter sp. LPB0142.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1850250 {ECO:0000313|EMBL:AOZ69946.1, ECO:0000313|Proteomes:UP000176562};
RN [1] {ECO:0000313|EMBL:AOZ69946.1, ECO:0000313|Proteomes:UP000176562}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0142 {ECO:0000313|EMBL:AOZ69946.1,
RC ECO:0000313|Proteomes:UP000176562};
RA Kim E., Yi H.;
RT "Rhodobacter sp. LPB0142, isolated from sea water.";
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}.
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DR EMBL; CP017781; AOZ69946.1; -; Genomic_DNA.
DR RefSeq; WP_068765815.1; NZ_CP017781.1.
DR AlphaFoldDB; A0A1D9MDL6; -.
DR STRING; 1850250.LPB142_11930; -.
DR KEGG; rhp:LPB142_11930; -.
DR Proteomes; UP000176562; 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:UP000176562};
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 14..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..191
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 387 AA; 41472 MW; 6D7EB527A45E900A CRC64;
MILHELISFD LLRLIWWGLL GVLLIGFALT DGFDMGVGAL LPFVAKGDTE RRVVINTVGP
VWEGNQVWFI LGGGAIFAAW PPLYAVSFSG FYLAMFAVLA ALILRPVGFK YRSKRPSPAW
RSGWDWALFV GGAVPALIFG VAVGNVLQGV PFELTEDLMP LYPGAFYAKF LGLLNPFALL
AGVVSLSMLL MHGAAWLTLK TEGAVQMRAR KIGTVAGGVA LLTYALAGLW LGAAIPGYHI
VSPVVANGPS NPLLTEVVRE GSWLSAYAAR PWIAVAPALG FLGIALATLG LRAGREVSTL
LFSKLGIFGV IASVGLTMFP FILPSSTMPS ASLTVWDASS SHLTLFVMLI VTVIFMPLIL
AYTAWVYKVL WGKVTVAEVT EHGDTLY
//
