TLCB_RICPR
ID TLCB_RICPR Reviewed; 507 AA.
AC Q9ZDF2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=ADP,ATP carrier protein 2;
DE AltName: Full=ADP/ATP translocase 2;
GN Name=tlcB; Synonyms=tlc2; OrderedLocusNames=RP377;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(1998).
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 -!- 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; AJ235271; CAA14836.1; -; Genomic_DNA.
DR PIR; B71695; B71695.
DR RefSeq; NP_220760.1; NC_000963.1.
DR RefSeq; WP_004597535.1; NC_000963.1.
DR AlphaFoldDB; Q9ZDF2; -.
DR STRING; 272947.RP377; -.
DR EnsemblBacteria; CAA14836; CAA14836; CAA14836.
DR KEGG; rpr:RP377; -.
DR PATRIC; fig|272947.5.peg.389; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; HIVWPIR; -.
DR Proteomes; UP000002480; 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;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..507
FT /note="ADP,ATP carrier protein 2"
FT /id="PRO_0000102581"
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; 58457 MW; 00DB2DFCC51D9D59 CRC64;
MNIVDSNCTI WHKARNSKFR HIVWPIRSYE LTKFIPMTLL MFFILLNQNL VRSIKDSFVV
TLISSEVLSF IKLWGEMPMG VLFVILYSKL CNIMTTEQVF RIITSTFLFF FAIFGFILFP
YKEFFHPNPE LINQYIIVLP HLKWFLIIWG QWSLVLFYIM GELWPVIVFT LLYWQLANKI
TKVEEAPRFY SFFTLFGQTN LLFSGTVIIY FAKSEHFLLP LFAHLNDTNE ILLKSFITVI
LISGLICLAL HKLIDKSVVE ADKNIKFKNQ RTDILKLSLL ESAKIILTSR YLGFICLLVM
SYSMSINLIE GLWMSKVKQL YPATKDFISY HGEVLFWTGV LTLVSAFLGS SLIRIYGWFW
GAIITPIMMF VAGVMFFSFT IFEQHLGNIV NTLGYSSPLV IIVFIGGLWH VFAKSVKYSL
FDATKEMVYI PLDNEIKTKG KAAVDVMGAK IGKSIGAIIQ FISFSIFPNA VHNDIAGLLM
VTFIIVCILW LYGVKVLSQN YNKMIKR