ID   A0A286GUV2_9ACTN        Unreviewed;       531 AA.
AC   A0A286GUV2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Cytochrome bd-I ubiquinol oxidase subunit 1 apoprotein {ECO:0000313|EMBL:SOD99308.1};
GN   ORFNames=SAMN06272739_2246 {ECO:0000313|EMBL:SOD99308.1};
OS   Blastococcus haudaquaticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1938745 {ECO:0000313|EMBL:SOD99308.1, ECO:0000313|Proteomes:UP000219482};
RN   [1] {ECO:0000313|Proteomes:UP000219482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44270 {ECO:0000313|Proteomes:UP000219482};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2017) 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, ECO:0000256|PIRNR:PIRNR006446}.
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DR   EMBL; OCNK01000002; SOD99308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286GUV2; -.
DR   OrthoDB; 9807042at2; -.
DR   Proteomes; UP000219482; Unassembled WGS sequence.
DR   GO; GO:0070069; C:cytochrome complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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:SF0; CYTOCHROME BD-I UBIQUINOL OXIDASE SUBUNIT 1; 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:UP000219482};
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        26..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        63..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        101..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        137..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        189..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        237..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        366..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        399..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   TRANSMEM        460..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT   REGION          493..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..524
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   531 AA;  58123 MW;  33067ADED9093949 CRC64;
     MDVVGLDVLD LDTLDVARWQ FGITTVYHFL MVPLTIGLGI LVAVMHTMWV RTDKPEWLRM
     TRFWGRVYLI NFVLGVATGL VQEFQFGLAW SEYSRFVGDV FGSLLALEAL LAFFLESTFL
     GLWIFGWGRI PKKVHLATLW AAVVGSIVSA YFIIAANSWM QHPVGVVTDD ATGRPRQVDF
     LAVLTNNTAL AAFSHAIVAA LMVAGALLVG IGLWHLRKRK LAQLPTTDTD HAVWRRSVRL
     GGWVSLAAFA LVALTGDWQG KLMYEQQPLK MSSAEALCET EAPASFSIFA WGKLGSNECD
     DVHSITVPYI LSYLAHGDFS TAVPGVNELQ EEYSAAYGET YPDDPSFGDK AGEPIDYTPV
     LAVTYWSFRL MIGMGAVSAA VAAYALWATR KGRVPTSRIG VYGSLLAVAA PFVGNATGWI
     FTEMGRQPFV VYPNPDVPVE DQIYFFTAQA VSPGISAGEV WTSLISLTVV YGALAVVELW
     LLSRFVRRGV TSGDGHPTPG FTPEPPDDGD DGPDRGAPRR DRDDDVLQFA Y
//