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Database: UniProt
Entry: Q6FA73_ACIAD
LinkDB: Q6FA73_ACIAD
Original site: Q6FA73_ACIAD 
ID   Q6FA73_ACIAD            Unreviewed;       488 AA.
AC   Q6FA73;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 69.
DE   SubName: Full=Putative permease {ECO:0000313|EMBL:CAG69040.1};
GN   OrderedLocusNames=ACIAD2247 {ECO:0000313|EMBL:CAG69040.1};
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter.
OX   NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG69040.1, ECO:0000313|Proteomes:UP000000430};
RN   [1] {ECO:0000313|EMBL:CAG69040.1, ECO:0000313|Proteomes:UP000000430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S.,
RA   Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P.,
RA   Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp.
RT   ADP1, a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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DR   EMBL; CR543861; CAG69040.1; -; Genomic_DNA.
DR   STRING; 62977.ACIAD2247; -.
DR   EnsemblBacteria; CAG69040; CAG69040; ACIAD2247.
DR   KEGG; aci:ACIAD2247; -.
DR   eggNOG; ENOG4105EW8; Bacteria.
DR   eggNOG; COG1953; LUCA.
DR   HOGENOM; HOG000165631; -.
DR   KO; K03457; -.
DR   OMA; MLVLLKF; -.
DR   Proteomes; UP000000430; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 1.10.4160.10; -; 1.
DR   InterPro; IPR001248; Pur-cyt_permease.
DR   InterPro; IPR038271; Pur-cyt_permease_sf.
DR   Pfam; PF02133; Transp_cyt_pur; 1.
PE   4: Predicted;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000430};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     38     60       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     66     87       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    122    143       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    163    181       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    193    211       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    231    252       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    272    294       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    314    335       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    356    374       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    386    405       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    434    454       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    460    478       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   488 AA;  53923 MW;  8A703B9E11150566 CRC64;
     MTNMQHESEA LIKPDYHPKL TNSDLAPLKK QTWTSYNIFA FWMSDVHSVG GYVTAGSLFA
     LGLNSWQVLV SLLIGIVIVQ FFANMIAKPS QKTSTPFPVI CRATFGVFGA NIPAVIRGII
     AVAWYGIQTY LASSAFIIII LKFWPEMTAY ADVKQHSFLG LSYLGWLGFM LLWVLQAVVF
     WSGMNSIRKF IDWAGPAVYV VMFAMAVWLV YEAGWSNINM NLGGVKYDGM DVIPVMIGAI
     ALVVSYFSGP VLNFGDFSRY GKSFEAVKFG NFLGLPVNFL AFSVLTVVCI AATLPIYGKL
     ITDPVEMVGQ LNNTFVVVLG CLTLMIATVG INIVANFVSP AFDFSNVSPN KISWRMGGMI
     AAVGSIFITP WNLFNNPQVI HYTIDVLGAL IGPLFGILIA DYYIVKKQKI EVDELYSINP
     HGKYWYQNGY NPKAIAALIP AAIIPILCVL LPQLHILANF SWFIGMFAGL IIYSLLSIKQ
     RVKIKSLI
//
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