TLCC_RICCN
ID TLCC_RICCN Reviewed; 501 AA.
AC Q92HP9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=ADP,ATP carrier protein 3;
DE AltName: Full=ADP/ATP translocase 3;
GN Name=tlcC; Synonyms=tlc3; OrderedLocusNames=RC0722;
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; AAL03260.1; -; Genomic_DNA.
DR PIR; B97790; B97790.
DR RefSeq; WP_010977341.1; NC_003103.1.
DR AlphaFoldDB; Q92HP9; -.
DR EnsemblBacteria; AAL03260; AAL03260; RC0722.
DR KEGG; rco:RC0722; -.
DR PATRIC; fig|272944.4.peg.822; -.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; HPNTIDY; -.
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..501
FT /note="ADP,ATP carrier protein 3"
FT /id="PRO_0000286472"
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 387..407
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; 57105 MW; 2EC589FAD865EA3B CRC64;
MLPPKIFFEK VKEIMWPIER KELKLFIPMA LMMLCILFNF GALRSIKDSL VVPSMGAEII
SFLKLWLVLP SCVIFTVLYV KLSNNLNFEY IFYIIVGSFL LFFLLFAYII YPNQDIYHPN
DEMINKLIAS YPNFKWFIKI GSQWSYALMY IFAELWSAVV INLMFWQFAN HIFDTSKAKR
FYPVLGMVGN IGLIIAGSVL VFFSSGQDVI DSELLPDSFN SSAGNAIMLQ PIMSIIVTAG
IIAMLLFRII NRFILTDSIN VLDAKKVTAK MKTKLSVIES IKLVIHSKYI GRIALLIICY
GLLINIVEGP WKAKIKELHP NTIDYVNFMG RFNIWMGISC VTFMIIGSNI LRRLGWLISA
LLTPIMLSIT GLMFFIFIIF IEEIGECFGD FNLLYAAIIV GAIQNILSKS SKYSLFDSTK
EMAYIPLSLE LRTKGKAAVE VIGTKFGKSL GAFIQSLIFI IIPTATFDSI IIYLLITFIV
MMSLWIWNVI KLNKEYVELC K