TLCE_RICBR
ID TLCE_RICBR Reviewed; 500 AA.
AC Q1RK92;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=ADP,ATP carrier protein 5;
DE AltName: Full=ADP/ATP translocase 5;
GN Name=tlcE; Synonyms=tlc5; OrderedLocusNames=RBE_0141;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04222.1; -; Genomic_DNA.
DR RefSeq; WP_011476837.1; NC_007940.1.
DR AlphaFoldDB; Q1RK92; -.
DR EnsemblBacteria; ABE04222; ABE04222; RBE_0141.
DR KEGG; rbe:RBE_0141; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; TSKEMLY; -.
DR OrthoDB; 427341at2; -.
DR Proteomes; UP000001951; 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..500
FT /note="ADP,ATP carrier protein 5"
FT /id="PRO_0000286485"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 500 AA; 57123 MW; ED6D5604AD7BABF0 CRC64;
MLSTSSSRPF KSKFRAAFWP IYNYELGKFI PMSALMFCIL FNQNILRILK DSILISEISA
EIAGFAKVYC VTPAAALFVI IYAKMINHLT FEKIFYYLTA FFIGFFVLFA FVIYPNIHIF
HVHPDYLADW MERYPHFKWY ISLIGNWGYI VYYSLAELWP NIFYVLLFWQ FANELTTTEE
AKRFYTLFSL FGNSSLILVG FLMMNLSSKE TIVKHFINIS DSKITLVQIS TILVTIVAVI
CCLLIRFISR NVFTNPLFYA KAKSGRSTSE RMGIIKSFKY IVKSKYLWLL LICSAAFGFA
INLVEAVWKA KIKELYPTVN TYAEFNSLYI LWTGVAIMVM TIIGNNVMRM HNWFVAAVIS
PVIIMVTGVL FFVLIVFDQK ILSLFDGAIL MSPLALAVSI GGIQNILAKG TKYSIWDTSR
EMLYIPLDQE LKTKGKAAVD VISAKVGKSS SGLVQSIIFT IIPTATFTSI SPVLMVVFTF
VCLAWIYAVR KIYFEYQKIA