ID H8L1Y1_FRAAD Unreviewed; 465 AA.
AC H8L1Y1;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Cytochrome bd-type quinol oxidase, subunit 1 {ECO:0000313|EMBL:AFC87236.1};
GN OrderedLocusNames=Fraau_2906 {ECO:0000313|EMBL:AFC87236.1};
OS Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Frateuria.
OX NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC87236.1, ECO:0000313|Proteomes:UP000005234};
RN [1] {ECO:0000313|Proteomes:UP000005234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Frateuria aurantia DSM 6220.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|PIRNR:PIRNR006446}. Membrane
CC {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; CP003350; AFC87236.1; -; Genomic_DNA.
DR RefSeq; WP_014404239.1; NC_017033.1.
DR AlphaFoldDB; H8L1Y1; -.
DR STRING; 767434.Fraau_2906; -.
DR KEGG; fau:Fraau_2906; -.
DR eggNOG; COG1271; Bacteria.
DR HOGENOM; CLU_030555_3_1_6; -.
DR OrthoDB; 9807042at2; -.
DR Proteomes; UP000005234; Chromosome.
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:SF14; CYTOCHROME BD2 SUBUNIT I; 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:UP000005234};
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 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 54..77
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 97..120
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 184..208
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 220..237
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 320..345
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 410..429
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT REGION 438..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 51845 MW; C31ECD7A3730BDB8 CRC64;
MEILDAFHLA RLQFAFTVSF HIMFPAFSIG MASFLAVLEG LWLKTRNEAY KDMFFFWTKI
FAVGFGMGVV SGVVMSYEFG TNWGGFSNIA GNITGPLLTY EVLTAFFLEA GFLGVMLFGW
EKVGPRAHFF STVMVAVGTL ISTFWILASN SFMQTPQGFG WENGKIIPLD WWKIVFNPSF
PFRLAHMAIA AFIVAGFIVA AVSAWHLLRG RRDEPVKKSF SMAMWILLIL CPVQIFVGDA
HGLNTREYQP AKIAAIEGLW ETEKGGTALN LFGLPDMQAE TTKYALKVPH LGSLILTHSW
DGEIRGLKEF PAQDRPYSPL IFWTFRIMAG LGMLMLLTAV VGFILRRAGK LYDCRWFQRF
VVCMGPSGIL ALLAGWITTE VGRQPWTVYG VLRTSDSLSP LDSQQVGTSL LIFVVVYFLV
FGTGIYYMLK MMKKGPTSGG DHHQHDHPGL DSSRPLSRPS DAIDG
//
