ID Q11AZ3_CHESB Unreviewed; 334 AA.
AC Q11AZ3;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Cytochrome bd quinol oxidase subunit 2 apoprotein {ECO:0000313|EMBL:ABG65432.1};
DE EC=1.10.3.- {ECO:0000313|EMBL:ABG65432.1};
GN OrderedLocusNames=Meso_4065 {ECO:0000313|EMBL:ABG65432.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG65432.1};
RN [1] {ECO:0000313|EMBL:ABG65432.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG65432.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) 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; CP000390; ABG65432.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11AZ3; -.
DR STRING; 266779.Meso_4065; -.
DR KEGG; mes:Meso_4065; -.
DR eggNOG; COG1294; Bacteria.
DR HOGENOM; CLU_049294_1_0_5; -.
DR OrthoDB; 9776710at2; -.
DR GO; GO:0005886; C:plasma membrane; 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; CYTOCHROME BD2 SUBUNIT II; 1.
DR PANTHER; PTHR43141:SF4; CYTOCHROME BD2 SUBUNIT II; 1.
DR Pfam; PF02322; Cyt_bd_oxida_II; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000313|EMBL:ABG65432.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 299..323
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 334 AA; 36761 MW; 22244B5931D39B6D CRC64;
MEWYLPAIWA GLIGTAVAMY VILDGFDLGI GILFPLTHEE EERDQMMNSV APFWDGNETW
LVLGGGGLWV AFPTAYSVIM PALYLPVMGM LLALVLRGVS FEFRWVAKPS HRMWDIAFAG
GSIIAAFLQG VILGGLLQGI QVADRQYAGG PLDWLTPFAI FVGLAVVAGY GLLGSTWLLM
RTIGPVQELG RRYAPIFLLA VLAGMGIVSL WTPLLIDRIA ERWFSLPNFY VLWPVPVAAA
LVGYGIWRWL AEGREGLPFF GAIVLFLLGY AGLVISTVPY LVPPHLTFWD TAAVPASQIF
LLIGTVFLLP LVFGYTIFVY WVFRAKVGPG EGYH
//
