TLCE_RICCN
ID TLCE_RICCN Reviewed; 499 AA.
AC Q92GI5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=ADP,ATP carrier protein 5;
DE AltName: Full=ADP/ATP translocase 5;
GN Name=tlcE; Synonyms=tlc5; OrderedLocusNames=RC1138;
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; AAL03676.1; -; Genomic_DNA.
DR PIR; B97842; B97842.
DR RefSeq; WP_010977709.1; NC_003103.1.
DR AlphaFoldDB; Q92GI5; -.
DR EnsemblBacteria; AAL03676; AAL03676; RC1138.
DR KEGG; rco:RC1138; -.
DR PATRIC; fig|272944.4.peg.1310; -.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; TSKEMLY; -.
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..499
FT /note="ADP,ATP carrier protein 5"
FT /id="PRO_0000286478"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 468..488
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 499 AA; 56919 MW; CDB73E469763E2AF CRC64;
MLSTSSRSFK NKFRAAFWPV HNYELGKFIP MSTLMFCILF NQNVLRILKD SILISEISAE
IAGFAKVYCV TPAAALFVII YAKMINYLTF EKIFYYLSAF FISFFVLFTF VIYPNIHIFH
VHPNNLADWM ERYPHFKWYI SLVGNWGYIV YYSLAELWPN IFYVLLFWQF ANELTTTEEA
KRFYTLFSLF GNSSLILVGF LMMNLSSEDT IIKKFMSISD SKITLVQVST TIVAIVAIIC
CLLVRFISKN VFTNPLFYAK AKSGRSTSER MGLIKSFKYI AKSKYLWLLL ICSAAFGFAI
NLVEAVWKAK IKELYPTVNT YAEFNSLYIL WTGVAIMVMT IIGNNIMRMH NWFVAAVISP
VIIMVTGILF FVLIVFDQQI LSLFDGAILM SPLALAVSIG GIQNILAKGT KYSIWDTSRE
MLYIPLDEEL KTKGKAAVDV ISAKVGKSSS GLVQSIIFTL VPTATFTLIS PILMVVFTFV
CLAWIYAVRK IYCEYQKIA