ID F5XWU2_RAMTT Unreviewed; 860 AA.
AC F5XWU2;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Candidate Cytochrome c oxidase polypeptide I (Cytochrome AA3 subunit 1) {ECO:0000313|EMBL:AEG91703.1};
GN Name=ctaD {ECO:0000313|EMBL:AEG91703.1};
GN OrderedLocusNames=Rta_06250 {ECO:0000313|EMBL:AEG91703.1};
OS Ramlibacter tataouinensis (strain ATCC BAA-407 / DSM 14655 / LMG 21543 /
OS TTB310).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=365046 {ECO:0000313|EMBL:AEG91703.1, ECO:0000313|Proteomes:UP000008385};
RN [1] {ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RA Barakat M., Ortet P., De Luca G., Jourlin-Castelli C., Ansaldi M., Py B.,
RA Fichant G., Coutinho P., Voulhoux R., Bastien O., Roy S., Marechal E.,
RA Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V., DuBow M.,
RA Barras F., Heulin T.;
RT "Genome of the cyst-dividing bacterium Ramlibacter tataouinensis.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEG91703.1, ECO:0000313|Proteomes:UP000008385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-407 / DSM 14655 / LMG 21543 / TTB310
RC {ECO:0000313|Proteomes:UP000008385};
RX PubMed=21912644; DOI=10.1371/journal.pone.0023784;
RA De Luca G., Barakat M., Ortet P., Fochesato S., Jourlin-Castelli C.,
RA Ansaldi M., Py B., Fichant G., Coutinho P.M., Voulhoux R., Bastien O.,
RA Marechal E., Henrissat B., Quentin Y., Noirot P., Filloux A., Mejean V.,
RA Dubow M.S., Barras F., Barbe V., Weissenbach J., Mihalcescu I.,
RA Vermeglio A., Achouak W., Heulin T.;
RT "The Cyst-Dividing Bacterium Ramlibacter tataouinensis TTB310 Genome
RT Reveals a Well-Stocked Toolbox for Adaptation to a Desert Environment.";
RL PLoS ONE 6:E23784-E23784(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00029368};
CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC {ECO:0000256|ARBA:ARBA00004673}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000245; AEG91703.1; -; Genomic_DNA.
DR RefSeq; WP_013899936.1; NC_015677.1.
DR AlphaFoldDB; F5XWU2; -.
DR STRING; 365046.Rta_06250; -.
DR KEGG; rta:Rta_06250; -.
DR PATRIC; fig|365046.3.peg.639; -.
DR eggNOG; COG0843; Bacteria.
DR eggNOG; COG1845; Bacteria.
DR HOGENOM; CLU_011899_6_0_4; -.
DR OrthoDB; 9803294at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000008385; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0015990; P:electron transport coupled proton transport; IEA:InterPro.
DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 1.
DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1.
DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom.
DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf.
DR InterPro; IPR000883; Cyt_C_Oxase_1.
DR InterPro; IPR000298; Cyt_c_oxidase-like_su3.
DR InterPro; IPR014241; Cyt_c_oxidase_su1_bac.
DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf.
DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx.
DR NCBIfam; TIGR02891; CtaD_CoxA; 1.
DR PANTHER; PTHR10422:SF35; CYTOCHROME BO(3) UBIQUINOL OXIDASE SUBUNIT 1; 1.
DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1.
DR SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 1.
DR PROSITE; PS50855; COX1; 1.
DR PROSITE; PS50253; COX3; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008385};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 64..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..479
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 499..520
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 632..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..703
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 723..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 754..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 796..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..859
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 47..558
FT /note="Cytochrome oxidase subunit I profile"
FT /evidence="ECO:0000259|PROSITE:PS50855"
FT DOMAIN 599..857
FT /note="Heme-copper oxidase subunit III family profile"
FT /evidence="ECO:0000259|PROSITE:PS50253"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 93055 MW; ED2FF300269441E3 CRC64;
MTAALGGAGA ALPASRGDPQ AAGVTPPLYR QSSGPDGLAR IAAAWAMPKR FGFLTEINNT
HIGVLYIATG FLFFLGAGVL ALLMRIQLAW PNNTFLDAAT YNQFFTMHGT VMMFLFAVPI
VEAVAVLLLP SMLGTRDMPF PRLSSLGYWC YAIGGAMVFS SLFLGVAPDG GWFMYPPLTG
ARYSPGINTD VWVLGLGFVE IAAVAAAVEL IVGILKTRAP GMTLGKMPIF AWYMLVTAGM
IMVGMPAVIA ADILLELERA FGMPFYDPTR GGEPLLWQHL FWLFAHPEVY IIFLPAAGMV
SMMLPSFART PLVGYSWVVL AALAVGFLSF GLWVHHMFTT GLPLLSLSFF SAASSAIAIP
MGIQVFAWIA TLWNGKPVLR VPMLFILGFL FIFVIGGLTG VMVAAVPYNW QVHDTYFVVA
HFHYVLIGGM VFPLFAALYY WIPAITGRML SERLGRWAFW LMFIGFNAAF LPMHLTGLLG
MPRRIYTYPG NLGWNTLNLV SSVFAFLFAA GVLVFVADFV RHRRSGQQAG HNPWDAPTLE
WMSGQPAHGF RSLMPITSLY PLWEHKALKD EELAGRGYLP DAPTQEREAL ATSPISAEPE
QIIRLPGPSW IPFLAATATA VAFAGMTVKS AAVGSAAGAV AAAAYLYWLW SMDKGLPREP
ADAGRGLALP LYRSDSGSVG WWGMTVLLIA DAVVLASFAF AYLFLWTAHP VAWPPDGSRL
PGFLGPAVIA ALVIGAWILF EAASRSNQRD RRSAASASLA AAAVLAAGAL IMGWMWLNSL
DIDPTRHSYG ASVWTLAGHV GLHVAIGAAM APWCIARQAL GMLDGWRSLT LHLCLLWWRF
TAPAAALTLI LITAFPHVVP
//
