TLCB_RICCN
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 25-MAY-2022, entry version 79.
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; Proteobacteria; 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}.
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DR EMBL; AE006914; AAL03060.1; -; Genomic_DNA.
DR PIR; B97765; B97765.
DR RefSeq; WP_010977161.1; NC_003103.1.
DR AlphaFoldDB; Q92I98; -.
DR EnsemblBacteria; AAL03060; AAL03060; RC0522.
DR KEGG; rco:RC0522; -.
DR PATRIC; fig|272944.4.peg.597; -.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; HIVWPIR; -.
DR Proteomes; UP000000816; 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 PANTHER; PTHR31187; PTHR31187; 1.
DR Pfam; PF03219; TLC; 1.
DR TIGRFAMs; TIGR00769; AAA; 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