TLCD_RICCN
ID TLCD_RICCN Reviewed; 511 AA.
AC Q92HV4;
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 4;
DE AltName: Full=ADP/ATP translocase 4;
GN Name=tlcD; Synonyms=tlc4; OrderedLocusNames=RC0666;
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; AAL03204.1; -; Genomic_DNA.
DR PIR; B97783; B97783.
DR RefSeq; WP_010977290.1; NC_003103.1.
DR AlphaFoldDB; Q92HV4; -.
DR EnsemblBacteria; AAL03204; AAL03204; RC0666.
DR KEGG; rco:RC0666; -.
DR PATRIC; fig|272944.4.peg.759; -.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; FLMTAIY; -.
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..511
FT /note="ADP,ATP carrier protein 4"
FT /id="PRO_0000286475"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
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 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 511 AA; 58036 MW; E194D7E21591EE02 CRC64;
MTINPSNVEN SSSKINSYFS KLTDYIWPIK RHEVSKFLFI TLLMFCILFI QNLIRALKDS
IVTTMIGAEI ISFLKFWGVM PSAFLMTAIY VKLVNKMKAE NIFYLIISIF LTFFALFAYV
IFPNHEMLHF SPVTVQNLMA SLPNLKWFIW LLSKWSFSLF YIIAELWPNV VFALLFWQFV
NNITTVEESK RFYPLFGLLS QTGIYLAGQF LENLSNINDY VTNKFALQSS FHTLSIQIIL
TIVLILGIIA IKTFWLLNHK VLDKEHMALL RFKAKKKSMT IAESFQMLLS SRHIRLIATL
LICYGIAINL VEGPWKAAAT KIYKTPTEYA AFIGSYLSYT GVFTILFVVL GSNIVRRLGW
FTAAVITPLI VFITGILFFA VNNFERFAGL IIANFILTDP ALIAITIGAI QNVLSKSSKY
TLFDSTKEMA YVPLDPEIKI KGKAAADVIG TKLGKSGSAF LQSLVFIILP SASYQSISTC
LMIIFIITCL TWLWATKALN KEYKNSIKFS Q