ID A0A068QQX0_9GAMM Unreviewed; 379 AA.
AC A0A068QQX0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cytochrome d ubiquinol oxidase subunit 2 {ECO:0000313|EMBL:CDG17046.1};
DE EC=1.10.3.- {ECO:0000313|EMBL:CDG17046.1};
GN Name=cydB {ECO:0000313|EMBL:CDG17046.1};
GN ORFNames=XDD1_1347 {ECO:0000313|EMBL:CDG17046.1};
OS Xenorhabdus doucetiae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG17046.1, ECO:0000313|Proteomes:UP000032721};
RN [1] {ECO:0000313|EMBL:CDG17046.1, ECO:0000313|Proteomes:UP000032721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA Genoscope - CEA;
RL Submitted (JUL-2013) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO704550; CDG17046.1; -; Genomic_DNA.
DR RefSeq; WP_045969657.1; NZ_VNHN01000008.1.
DR AlphaFoldDB; A0A068QQX0; -.
DR STRING; 351671.XDD1_1347; -.
DR KEGG; xdo:XDD1_1347; -.
DR HOGENOM; CLU_049294_0_0_6; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000032721; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; 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 Oxidoreductase {ECO:0000313|EMBL:CDG17046.1};
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..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 379 AA; 42194 MW; E66CC50E4C618AF4 CRC64;
MLDYDVLRFI WWLLIGVLLI GFTVTDGFDM GVGILLRIIG KNDTERRIMI NSIAPHWDGN
QVWLITAGGA LFAAWPMVYA AAFSGFYVAM ILVLAALFFR PVGFDYRSKL ENSKWRNMWD
WGLVIGSFVP ALVIGVAFGN LLQGVPLAVD TYLRVSYEGS FFGLLNPYGL LAGVISLMMI
VTQGATYLQM RTTGELHLRS RTATHVCAAV TAIAFLLAGI WLIYGIDGYV VTGGLDVNAA
SNPLHKEVVQ QAGAWLTNFN HYPILWAIPA LGVLLPLLTI LTTWMDKGAW AFFFSSLTVA
CIILTSGIAM FPFVMPSSLD PNVSLTMWDA TSSQWTLQIM FVVALIFVPI VLSYTIWCYY
KTFGRLDKNY IENNKHSLY
//
