TLCA_RICPR
ID TLCA_RICPR Reviewed; 498 AA.
AC P19568;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=ADP,ATP carrier protein 1;
DE AltName: Full=ADP/ATP translocase 1;
GN Name=tlcA; Synonyms=tlc, tlc1; OrderedLocusNames=RP053;
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 [GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=2555259; DOI=10.1016/0378-1119(89)90291-6;
RA Williamson L.R., Plano G.V., Winkler H.H., Krause D.C., Wood D.O.;
RT "Nucleotide sequence of the Rickettsia prowazekii ATP/ADP translocase-
RT encoding gene.";
RL Gene 80:269-278(1989).
RN [2]
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).
RN [3]
RP TOPOLOGY.
RX PubMed=1904433; DOI=10.1128/jb.173.11.3389-3396.1991;
RA Plano G.V., Winkler H.H.;
RT "Identification and initial topological analysis of the Rickettsia
RT prowazekii ATP/ADP translocase.";
RL J. Bacteriol. 173:3389-3396(1991).
RN [4]
RP TOPOLOGY.
RX PubMed=2165754; DOI=10.1111/j.1749-6632.1990.tb42247.x;
RA Plano G.V., Wood D.O., Winkler H.H.;
RT "Rickettsia prowazekii and ATP/ADP translocase. Analysis of gene fusions
RT encoding beta-galactosidase-ATP/ADP translocase fusion proteins.";
RL Ann. N. Y. Acad. Sci. 590:397-407(1990).
RN [5]
RP TOPOLOGY.
RX PubMed=9917392; DOI=10.1006/jmbi.1998.2412;
RA Alexeyev M.F., Winkler H.H.;
RT "Membrane topology of the Rickettsia prowazekii ATP/ADP translocase
RT revealed by novel dual pho-lac reporters.";
RL J. Mol. Biol. 285:1503-1513(1999).
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; M28816; AAA26382.1; -; Genomic_DNA.
DR EMBL; AJ235270; CAA14524.1; -; Genomic_DNA.
DR PIR; JQ0026; JQ0026.
DR RefSeq; NP_220447.1; NC_000963.1.
DR RefSeq; WP_004599717.1; NC_000963.1.
DR AlphaFoldDB; P19568; -.
DR STRING; 272947.RP053; -.
DR TCDB; 2.A.12.1.1; the atp:adp antiporter (aaa) family.
DR EnsemblBacteria; CAA14524; CAA14524; CAA14524.
DR GeneID; 57569181; -.
DR KEGG; rpr:RP053; -.
DR PATRIC; fig|272947.5.peg.54; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; RKVIWPI; -.
DR Proteomes; UP000002480; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:CACAO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IEA:InterPro.
DR GO; GO:0015867; P:ATP transport; IDA:CACAO.
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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..498
FT /note="ADP,ATP carrier protein 1"
FT /id="PRO_0000102580"
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; 56822 MW; D3C450D2BC0BE53E CRC64;
MSTSKSENYL SELRKIIWPI EQYENKKFLP LAFMMFCILL NYSTLRSIKD GFVVTDIGTE
SISFLKTYIV LPSAVIAMII YVKLCDILKQ ENVFYVITSF FLGYFALFAF VLYPYPDLVH
PDHKTIESLS LAYPNFKWFI KIVGKWSFAS FYTIAELWGT MMLSLLFWQF ANQITKIAEA
KRFYSMFGLL ANLALPVTSV VIGYFLHEKT QIVAEHLKFV PLFVIMITSS FLIILTYRWM
NKNVLTDPRL YDPALVKEKK TKAKLSFIES LKMIFTSKYV GYIALLIIAY GVSVNLVEGV
WKSKVKELYP TKEAYTIYMG QFQFYQGWVA IAFMLIGSNI LRKVSWLTAA MITPLMMFIT
GAAFFSFIFF DSVIAMNLTG ILASSPLTLA VMIGMIQNVL SKGVKYSLFD ATKNMAYIPL
DKDLRVKGQA AVEVIGGRLG KSGGAIIQST FFILFPVFGF IEATPYFASI FFIIVILWIF
AVKGLNKEYQ VLVNKNEK
