ID A0A1M6MKU1_9BACL Unreviewed; 454 AA.
AC A0A1M6MKU1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Cytochrome d ubiquinol oxidase subunit I {ECO:0000313|EMBL:SHJ83893.1};
GN ORFNames=SAMN05443507_10493 {ECO:0000313|EMBL:SHJ83893.1};
OS Alicyclobacillus montanus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1830138 {ECO:0000313|EMBL:SHJ83893.1, ECO:0000313|Proteomes:UP000184016};
RN [1] {ECO:0000313|Proteomes:UP000184016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA-503 {ECO:0000313|Proteomes:UP000184016};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR006446}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1
CC family. {ECO:0000256|ARBA:ARBA00009819, ECO:0000256|PIRNR:PIRNR006446}.
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DR EMBL; FRAF01000004; SHJ83893.1; -; Genomic_DNA.
DR RefSeq; WP_072873169.1; NZ_FRAF01000004.1.
DR AlphaFoldDB; A0A1M6MKU1; -.
DR STRING; 1830138.SAMN05443507_10493; -.
DR OrthoDB; 9807042at2; -.
DR Proteomes; UP000184016; Unassembled WGS sequence.
DR GO; GO:0070069; C:cytochrome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR InterPro; IPR002585; Cyt-d_ubiquinol_oxidase_su_1.
DR PANTHER; PTHR30365:SF3; CYTOCHROME BD MENAQUINOL OXIDASE SUBUNIT I-RELATED; 1.
DR PANTHER; PTHR30365; CYTOCHROME D UBIQUINOL OXIDASE; 1.
DR Pfam; PF01654; Cyt_bd_oxida_I; 1.
DR PIRSF; PIRSF006446; Cyt_quinol_oxidase_1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR006446};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR006446};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006446};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Reference proteome {ECO:0000313|Proteomes:UP000184016};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006446}.
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 58..80
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 86..113
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 125..143
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 181..204
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 317..342
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 354..380
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 404..427
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
SQ SEQUENCE 454 AA; 50400 MW; 278F2D48BD5F5579 CRC64;
MDHVHLARAL FGMSLGFHII YATLGVGIPF MVTVAEVSYA LTGDHDYAVM AKRWTRGFTV
LLAVSITTGT TVALQLSLLW PKFMQLVGQV IALPFLIEVF AFFLEALFMS IYVYAADRIP
RRWRILSVLL VAIGAAASAL LITDANAFMN APQGFRLVNG RAVDIHPWQA VFNRALPTSD
FHVMMTAYMA VGFVTAAIAA YGLLKKSHTE RERKHQYKAL MLSLALGGLF GLVAAISGDS
AGKYLAKYQP EKLAVAEGLF QTQAHAPLVI GGWVSGTRQD VIGGIKIPDF LSWLATERLD
GVVLGLNSFP RDTWPPLFLH LFFDGMVGIG TLLIFFAIFA WLVKTLRKQH EYPFPNWMLG
VTVLTGPLAM LAIELGWIYA CIGRQPWIIY HVMRTADAVT SAPYVGWMFV LFMLLYLLLA
IGSITVLRFY FSRHPLSDDI DPSAPKPRRV VWLP
//