ID TLCA_RICFE Reviewed; 498 AA. AC Q4UN85; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2005, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=ADP,ATP carrier protein 1; DE AltName: Full=ADP/ATP translocase 1; GN Name=tlcA; Synonyms=tlc1; OrderedLocusNames=RF_0122; OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=315456; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-1525 / URRWXCal2; RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248; RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., RA Parinello H., Claverie J.-M., Raoult D.; RT "The genome sequence of Rickettsia felis identifies the first putative RT conjugative plasmid in an obligate intracellular parasite."; RL PLoS Biol. 3:1-12(2005). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000053; AAY60973.1; -; Genomic_DNA. DR AlphaFoldDB; Q4UN85; -. DR STRING; 315456.RF_0122; -. DR KEGG; rfe:RF_0122; -. DR eggNOG; COG3202; Bacteria. DR HOGENOM; CLU_023964_0_1_5; -. DR OrthoDB; 19786at2; -. DR Proteomes; UP000008548; Chromosome. 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 NCBIfam; TIGR00769; AAA; 1. DR PANTHER; PTHR31187; -; 1. DR PANTHER; PTHR31187:SF13; ADP,ATP CARRIER PROTEIN 1, CHLOROPLASTIC; 1. DR Pfam; PF03219; TLC; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 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_0000286467" 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; 56708 MW; C390C2E20C3C58C4 CRC64; MNTPKSDNYL SELRKVIWPI EKYENKKFLP MAFMMFCILL NYSTLRSIKD GFVVTDIGAE AISFLKTYIV LPSAVIAMVI YVKLCDILKQ ENVFYVITSF FLGYFALFAF VLYPYPDLVH PDPETIESLS LAYPNFKWFI RIVGKWSFAS FYTMAELWGT MMLSLLFWQF ANQITKTDEA KRFYSMFGLL ANLALPVTSV IIGYFLHEKT QIVAEHLKFV PLFVIMITSS FLVILTYRWM NRNVLTDPRL YDPALVKEKK AKAKMSLIDS FKMIFTSKYV GYIALLLIAY GISVNLVEGV WKSKVKELYP TKEAYTIYMG KFQFYQGWVA IAFMLIGSNI LRKVSWLAAA MITPLMMLIT GAAFFAFIFF DSVIAMHLTG ILASGPLALA VMIGMIQNVL SKGVKYSLFD ATKNMAYIPL DKDLRVKGQA AVEVIGGRFG KSGGAIIQST FFILFPAFGF VEATPYFASI FFVIVILWIY AVKGLNKEYQ VLVNKTEK //