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 03-AUG-2022, entry version 78.
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}.
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DR EMBL; AE017197; AAU03565.1; -; Genomic_DNA.
DR RefSeq; WP_011190552.1; NC_006142.1.
DR AlphaFoldDB; Q68XS7; -.
DR STRING; 257363.RT0079; -.
DR EnsemblBacteria; AAU03565; AAU03565; RT0079.
DR KEGG; rty:RT0079; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; RKVIWPI; -.
DR OrthoDB; 427341at2; -.
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_bac_type.
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;
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 BINDING 436..442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
