TLCA_RICBR
ID TLCA_RICBR Reviewed; 498 AA.
AC Q1RGS8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=ADP,ATP carrier protein 1;
DE AltName: Full=ADP/ATP translocase 1;
GN Name=tlcA; Synonyms=tlc1; OrderedLocusNames=RBE_1355;
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; ABE05436.1; -; Genomic_DNA.
DR RefSeq; WP_011478005.1; NC_007940.1.
DR AlphaFoldDB; Q1RGS8; -.
DR STRING; 336407.RBE_1355; -.
DR EnsemblBacteria; ABE05436; ABE05436; RBE_1355.
DR KEGG; rbe:RBE_1355; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; RKVIWPI; -.
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 InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR31187; PTHR31187; 1.
DR Pfam; PF03219; TLC; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00769; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Disulfide bond; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..498
FT /note="ADP,ATP carrier protein 1"
FT /id="PRO_0000286481"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 55..67
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 89..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 114..147
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 169..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 206..218
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 240..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 301..320
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 342..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 370..379
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 401..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 460..465
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 487..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 436..442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT DISULFID 37..85
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 56416 MW; 62D6A38FB3207AD8 CRC64;
MSTTKSDNYI SELRKVIWPI ERYENKKFLP MAFMMFCILL NYSTLRSIKD GFVVTDIGAE
AISFLKTYIV LPSAVIAMIV YVKLCDILKQ ENVFYVITSF FLAYFALFAF VLYPNPDLVH
PNPEAIESLS LAYPNFKWFI RIVGKWSFAS FYTMAELWGT LMLSLLFWQF ANQITKTDEA
KRFYSMFGLL ANLALPVTSL IIGYFLHEKT QIVAEHLKFT PLFVIMIISS LAVILTYRWM
NKNVLTDPKL YDPALVKGKK AKAKMSLIES FKMIFTSKYV GYIALLLIAY GISVNLVEGV
WKSKLKELHP TKEAYTMYMG QFQAYQGWVA IAFMIIGSNI LRKVSWLTAA MITPLMMLIT
GIAFFAFIFF DSVIAMYLTG ILASGPLALA VMIGTIQNVL SKGVKYSLFD ATKNMAYIPL
DKDLRVKGQA AVEVIGGRFG KSGGAIIQST FFIIFPALGF VEATPYFASI FFVIVILWIY
AVKGLNKEYQ VLVNNTEK