TLCB_RICTY
ID TLCB_RICTY Reviewed; 507 AA.
AC Q68WZ7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=ADP,ATP carrier protein 2;
DE AltName: Full=ADP/ATP translocase 2;
GN Name=tlcB; Synonyms=tlc2; OrderedLocusNames=RT0366;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03845.1; -; Genomic_DNA.
DR RefSeq; WP_011190829.1; NC_006142.1.
DR AlphaFoldDB; Q68WZ7; -.
DR STRING; 257363.RT0366; -.
DR EnsemblBacteria; AAU03845; AAU03845; RT0366.
DR KEGG; rty:RT0366; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; HIVWPIR; -.
DR OrthoDB; 427341at2; -.
DR Proteomes; UP000000604; 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_0000286471"
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; 58374 MW; B8895F62706AB8F1 CRC64;
MNIVDSNCTI WHKARNSKFR HIVWPIRSYE LTKFIPMALL MFFILLNQNL VRSLKDSFVV
TLISSEVLSF IKLWGEMPMG VLFVILYSKL CNIMTTEQVF RIITGTFLFF FTIFGFILFP
YKEFFHPDPE LINQYITVLP HLKWFLIIWG QWSLVLFYIM GELWPVIVFT LLYWQLANKI
TKVEEAPRFY SFFTLFGQTN LLFSGTVIIY FAKSEHFLLP LFAHLNDTNE ILLKSFITVI
LLSGLICLAL HKLIDKSVVE ADKNIKFKNQ RTDILKLSLI ESAKIILTSR YLGFICLLVM
SYSMSINLIE GLWMSKVKQL YPATKDFISY HGEVLFWTGV LTLVSAFLGS SLIRIYGWFW
GAIITPIMMF VAGVIFFSFT IFENHLGNIV NTLGYSSPLV IIVFIGGLWH VFSKSVKYSL
FDATKEMVYI PLDNEIKTKG KAAVDVIGAK IGKSIGAVIQ FISFSIFPNA VHNDIAGLLM
FTFIIVCILW IYGVKVLSQY NNKMIQN