ID A0A2P8VPM3_9ENTR Unreviewed; 379 AA.
AC A0A2P8VPM3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Cytochrome d ubiquinol oxidase subunit II {ECO:0000313|EMBL:PSN09516.1};
GN Name=cydB {ECO:0000313|EMBL:PSN09516.1};
GN ORFNames=C7G83_01850 {ECO:0000313|EMBL:PSN09516.1};
OS Siccibacter turicensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Siccibacter.
OX NCBI_TaxID=357233 {ECO:0000313|EMBL:PSN09516.1, ECO:0000313|Proteomes:UP000240212};
RN [1] {ECO:0000313|EMBL:PSN09516.1, ECO:0000313|Proteomes:UP000240212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6100069499-17 {ECO:0000313|EMBL:PSN09516.1,
RC ECO:0000313|Proteomes:UP000240212};
RA Lepuschitz S., Pekard-Amenitsch S., Haunold R., Schill S., Mach R.,
RA Allerberger F., Ruppitsch W., Forsythe S.J.;
RT "Draft genome sequence of the first documented clinical Siccibacter
RT turicensis isolate in Austria.";
RL Submitted (MAR-2018) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PSN09516.1}.
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; PYEP01000001; PSN09516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8VPM3; -.
DR STRING; 1388748.GCA_000463155_01566; -.
DR OrthoDB; 9776710at2; -.
DR Proteomes; UP000240212; 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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..182
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..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..315
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 379 AA; 42475 MW; DE2AC78082BF5509 CRC64;
MFDYEVLRFI WWLLVGILLI GFAVTDGFDM GVGMLSRIIG RNDVERRIMV NSIAPHWDGN
QVWLITAGGA LFAAWPMVYA AAFSGFYVAM ILVLASLFFR PVGFDYRSKI EDMRWRNMWD
WGIFIGSFVP PLVIGVAFGN LLQGVPFHID SDLRLFYTGN FFQLLNPFGL LAGVVSVSMI
LAQGATYLQM RTVGEVHLRS RAVAQIAALV MMVCFVLAGV WVMYGIDGYV VTSELNRHAA
SNPLTKEVAR QAGAWFTNFN NMPVLWAIPA LGVVLPLLTV LFSRMEKGAW AFLFSSLTLA
CVILTAGIAM FPFVMPSSTM LNASLTMWDA TSTQRTLNLM TWVAAVFVPI ILLYSAWCYW
KMFGRITKEH IESNTHSLY
//
