TLCB_RICFE
ID TLCB_RICFE Reviewed; 507 AA.
AC Q4ULY0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=ADP,ATP carrier protein 2;
DE AltName: Full=ADP/ATP translocase 2;
GN Name=tlcB; Synonyms=tlc2; OrderedLocusNames=RF_0592;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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; CP000053; AAY61443.1; -; Genomic_DNA.
DR RefSeq; WP_011270922.1; NC_007109.1.
DR AlphaFoldDB; Q4ULY0; -.
DR EnsemblBacteria; AAY61443; AAY61443; RF_0592.
DR KEGG; rfe:RF_0592; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; HIVWPIR; -.
DR OrthoDB; 427341at2; -.
DR Proteomes; UP000008548; 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_0000286469"
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; 58412 MW; 964C7A9E05E4182F CRC64;
MDAVDSNFTI WNKARNSKFR HIVWPIRSYE LTKFIPMVLL MFFILLNQNL VRSIKDSFVV
TLISSEVLSF IKLWGEMPMG ILFVILYSKL CNIMTTEQVF RIITGTFLFF FAIFGFILFP
YREFFHPDPE LIKHYITVLP HLKWFLIIWG QWSLVLFYIM GELWPVIVFT LLYWQLANKI
TKVEEAPRFY SFFTLFGQTN LLISGTVIIY FAKSEHFLLP LFSHLNDTNE ILLKSFITVI
LISGLICLAL HKLIDKSVVE ADKNIKFKNQ RTDILKLSLV ESAKVILTSR YLGFICLLVM
SYSMSISLIE GLWMSKVKQL YPATKDFISY HGEVFFWTGV LTLVSAFLGS SLIRICGWFW
GAIITPIMMF GAGVMFFSFT VFENHLENIV NTLGYSLPLV VIVFIGGLWH VLSKSVKYSL
FDATKEMVYI PLDSEMKTKG KAAVDVMGTK IGKSIGAIIQ FISFSIFPNA VHNDIAGLLM
FSFVIVCLLW LYGVKVLSEQ YNKMIKR