ID TLCB_RICCN Reviewed; 507 AA. AC Q92I98; DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 86. DE RecName: Full=ADP,ATP carrier protein 2; DE AltName: Full=ADP/ATP translocase 2; GN Name=tlcB; Synonyms=tlc2; OrderedLocusNames=RC0522; OS Rickettsia conorii (strain ATCC VR-613 / Malish 7). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group. OX NCBI_TaxID=272944; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-613 / Malish 7; RX PubMed=11557893; DOI=10.1126/science.1061471; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). 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; AE006914; AAL03060.1; -; Genomic_DNA. DR PIR; B97765; B97765. DR RefSeq; WP_010977161.1; NC_003103.1. DR AlphaFoldDB; Q92I98; -. DR GeneID; 927640; -. DR KEGG; rco:RC0522; -. DR PATRIC; fig|272944.4.peg.597; -. DR HOGENOM; CLU_023964_0_1_5; -. DR Proteomes; UP000000816; 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..507 FT /note="ADP,ATP carrier protein 2" FT /id="PRO_0000286470" FT TRANSMEM 31..51 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 67..87 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 99..119 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 130..150 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 154..174 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 192..212 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 231..251 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 292..312 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 333..353 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 357..377 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 393..413 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 451..471 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 474..494 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 507 AA; 58365 MW; 49A92CD91E300C70 CRC64; MDSVDSNFTI WNKARNSKFR HIVWPIRSYE LTKFIPMALL MFFILLNQNL VRSIKDSFVV TLISSEVLSF IKLWGEMPMG ILFVIFYSKL CNIMTTEQVF RIITGTFLFF FAIFGFILFP YREFFHPDPE LIKHYITVLP HLKWFLIIWG QWSLVLFYIM GELWPVIVFT LLYWQLANKI TKVEEAPRFY SFFTLFGQTN LLISGTVIIY FAKSEHFLLP LFSHLNDTNE ILLKSFITVI LISGLICLAL HKLIDKSVVE ADKNIKFKNQ RMDILKLSLV DSAKVILTSR YLGFICLLVM SYSMSISLIE GLWMSKVKQL YPATKDFIAY HGKVFFWTGI LTLVSAFLGS SLIRICGWFW GAIITPIMMF GAGVMFFSFT VFENHLGNIV NTLGYSAPLV VIVFIGGLWH VLSKSVKYSL FDATKEMVYI PLDSEMKTKG KAAVDVMGAK IGKSIGAIIQ FISFSIFPNA IHNDIAGLLM FSFIIVCLLW LYGVKVLSKY YNKMIQR //