(data stored in SCRATCH3701 zone)

SWISSPROT: TLCA_RICTY

ID   TLCA_RICTY              Reviewed;         498 AA.
AC   Q68XS7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 72.
DE   RecName: Full=ADP,ATP carrier protein 1;
DE   AltName: Full=ADP/ATP translocase 1;
GN   Name=tlcA; Synonyms=tlc1; OrderedLocusNames=RT0079;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Provides the rickettsial cell with host ATP in exchange for
CC       rickettsial ADP. This is an obligate exchange system. This energy
CC       acquiring activity is an important component of rickettsial parasitism
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ADP/ATP translocase tlc family.
CC       {ECO:0000305}.
DR   EMBL; AE017197; AAU03565.1; -; Genomic_DNA.
DR   RefSeq; WP_011190552.1; NC_006142.1.
DR   STRING; 257363.RT0079; -.
DR   EnsemblBacteria; AAU03565; AAU03565; RT0079.
DR   KEGG; rty:RT0079; -.
DR   eggNOG; ENOG4105E7T; Bacteria.
DR   eggNOG; COG3202; LUCA.
DR   HOGENOM; HOG000238123; -.
DR   KO; K03301; -.
DR   OMA; RKVIWPI; -.
DR   OrthoDB; 427341at2; -.
DR   BioCyc; RTYP257363:G1G0L-80-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR   InterPro; IPR004667; ADP_ATP_car.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR31187; PTHR31187; 1.
DR   Pfam; PF03219; TLC; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00769; AAA; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68XS7.
DR   SWISS-2DPAGE; Q68XS7.
KW   ATP-binding; Cell membrane; Disulfide bond; Membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..498
FT                   /note="ADP,ATP carrier protein 1"
FT                   /id="PRO_0000286468"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        55..67
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        89..92
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        114..147
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        169..184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        206..218
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        240..279
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        301..320
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        342..348
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        370..379
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        401..438
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        460..465
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   TOPO_DOM        487..498
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   NP_BIND         436..442
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..85
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   498 AA;  56882 MW;  20C82BF035662AF6 CRC64;
     MSTSKSENYL SELRKIIWPI EQHENKKFLP LAFMMFCILL NYSTLRSIKD GFVVTDIGTE
     SISFLKTYIV LPSAVIAMVI YVKLCDILKQ ENIFYVITSF FLGYFALFAF VLYPYPDLVH
     PDHKTIESLS LAYPNFKWFI KIVGKWSFAS FYTIAELWGT MMLSLLFWQF ANQITKITEA
     KRFYSMFGLL ANLALPVTSV VIGYFLHEKT QIVSEHLKFI PLFVIMITSS FLIILTYRWM
     NKNVLTDPRL YDPTLVKEKK AKAKLSFIES FKMIFTSKYV GYIALLIIAY GVSVNLVEGV
     WKSKVKELYP TKEAYTIYMG QFQFYQGWVA IAFMLIGSNI LRKVSWLTAA MITPLMMFIT
     GAAFFSFIFF DSVIAMNLTG ILASSPLTLA VMFGMIQNVL SKGVKYSLFD ATKNMAYIPL
     DKDLRVKGQA AVEVIGGRLG KSGGAIIQST FFILFPAFGF IEATPYFASI FFIIVILWIF
     AVKGLNKEYQ VLVNKNEN
//

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