ID A0A0N0TIN5_9ACTN Unreviewed; 416 AA.
AC A0A0N0TIN5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Cytochrome BD oxidase subunit I {ECO:0000313|EMBL:KOX05696.1};
GN ORFNames=ADK66_24945 {ECO:0000313|EMBL:KOX05696.1};
OS Micromonospora sp. NRRL B-16802.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1415541 {ECO:0000313|EMBL:KOX05696.1, ECO:0000313|Proteomes:UP000037709};
RN [1] {ECO:0000313|EMBL:KOX05696.1, ECO:0000313|Proteomes:UP000037709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16802 {ECO:0000313|EMBL:KOX05696.1,
RC ECO:0000313|Proteomes:UP000037709};
RA Noorani M.;
RL Submitted (JUL-2015) 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 1
CC family. {ECO:0000256|ARBA:ARBA00009819}.
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:KOX05696.1}.
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DR EMBL; LGEB01000086; KOX05696.1; -; Genomic_DNA.
DR RefSeq; WP_053659320.1; NZ_LGEB01000086.1.
DR AlphaFoldDB; A0A0N0TIN5; -.
DR STRING; 1415541.ADK66_24945; -.
DR PATRIC; fig|1415541.3.peg.5228; -.
DR OrthoDB; 9807042at2; -.
DR Proteomes; UP000037709; Unassembled WGS sequence.
DR GO; GO:0070069; C:cytochrome complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR InterPro; IPR002585; Cyt-d_ubiquinol_oxidase_su_1.
DR PANTHER; PTHR30365:SF14; CYTOCHROME BD2 SUBUNIT I; 1.
DR PANTHER; PTHR30365; CYTOCHROME D UBIQUINOL OXIDASE; 1.
DR Pfam; PF01654; Cyt_bd_oxida_I; 2.
DR PIRSF; PIRSF006446; Cyt_quinol_oxidase_1; 2.
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 20..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 394..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 45200 MW; 469031B862F863C6 CRC64;
MDTLLLARLQ FATTTSIHFL FVVVTLGLVT LLVGMQTAWV LTGNPKWERL TRYWGQLYVI
NYVLGIATGI VMEFQFGLNW SGLSRYVGNV FGAPLAIETL VAFFLESTFL GMWIFGWHRL
RKGVHLALLW GVALTAYASA FWIMVANSWL QNPVGYEVRD GIAHLTDFGA LLTNPSLGMA
FGHVVSAALL VGGMLMAAVS AWHLIRRTPD FLLFRTSLRI GLVTAALAIT LVQGFGFAQF
GAVGSVQPTK FGQGPEAQAL VAEWTARFGP GDYAPPVLAN VGLGFMILIG LALGCVWLLL
PLLFRDWIIR LRFPLWLTLL ALPLPFVAVI LGWIAREVGR QPWVAYGLLP TEQAVSPVGA
PVMLTSLIGF SLLLGTLAVT NWVLLARHAA RGAADPALGR PPAPSSEPAR PEPALF
//
