ID TLCC_RICTY Reviewed; 501 AA. AC Q68WQ3; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 27-MAR-2024, entry version 79. DE RecName: Full=ADP,ATP carrier protein 3; DE AltName: Full=ADP/ATP translocase 3; GN Name=tlcC; Synonyms=tlc3; OrderedLocusNames=RT0464; OS Rickettsia typhi (strain ATCC VR-144 / Wilmington). OC Bacteria; Pseudomonadota; 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}. 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; AE017197; AAU03939.1; -; Genomic_DNA. DR RefSeq; WP_011190922.1; NC_006142.1. DR AlphaFoldDB; Q68WQ3; -. DR KEGG; rty:RT0464; -. DR eggNOG; COG3202; Bacteria. DR HOGENOM; CLU_023964_0_1_5; -. DR OrthoDB; 19786at2; -. DR Proteomes; UP000000604; 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 NCBIfam; TIGR00769; AAA; 1. DR PANTHER; PTHR31187; -; 1. DR PANTHER; PTHR31187:SF13; ADP,ATP CARRIER PROTEIN 1, CHLOROPLASTIC; 1. DR Pfam; PF03219; TLC; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..501 FT /note="ADP,ATP carrier protein 3" FT /id="PRO_0000286474" FT TRANSMEM 23..43 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 59..79 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 90..110 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 146..166 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 183..203 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 227..247 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 293..313 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 326..346 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 361..381 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 383..403 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 446..466 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 470..490 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 501 AA; 57193 MW; 5145AEB78D2B2F23 CRC64; MLPPKIFFEK FKEIIWPIER KELKLFIPMA LMMLCILFNF GALRSIKDSL VVPSMGAEII SFLKLWLVLP SCVIFTVLYV KLSNKLNFEY IFYSIVGTFL LFFLLFAYII YPNQDIYHPN DAMINNLIAS YPNLKWFIKI GSKWSYALMY IFSELWSAVV INLMFWQFAN HIFDTAKAKR FYPVLGMIGN IGLIIAGSVL VFFSSGQYII DSELLTDSFN SSSCNSIILQ PIISIIVTAG IIAMFLFRII NRFILTNAIN VLDVKKAAAR TKTKLALIES IKLIIHSKYI GRIALLIICY GLLINIVEGP WKAKIKELHP NTIDYVNFMG MFNIWMGISC VTFMIIGSNI LRRLGWLISA LLTPIMLSIT GFIFFIFIIF IEEIGTCFGD FNLLYVAIIV GAIQNILSKS SKYSLFDSTK EMAYIPLSLE LRTKGKAAVE VIGTKFGKSL GAFIQSLIFI IIPTATFDSI IIYLLVIFIV MMNLWIWNII KLNKEYIKLC K //