TLCC_RICPR
ID TLCC_RICPR Reviewed; 501 AA.
AC Q9ZD67;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=ADP,ATP carrier protein 3;
DE AltName: Full=ADP/ATP translocase 3;
GN Name=tlcC; Synonyms=tlc3; OrderedLocusNames=RP477;
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; CAA14932.1; -; Genomic_DNA.
DR PIR; B71707; B71707.
DR RefSeq; NP_220856.1; NC_000963.1.
DR RefSeq; WP_004599498.1; NC_000963.1.
DR AlphaFoldDB; Q9ZD67; -.
DR STRING; 272947.RP477; -.
DR EnsemblBacteria; CAA14932; CAA14932; CAA14932.
DR KEGG; rpr:RP477; -.
DR PATRIC; fig|272947.5.peg.489; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; HPNTIDY; -.
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..501
FT /note="ADP,ATP carrier protein 3"
FT /id="PRO_0000102582"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 446..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 501 AA; 57182 MW; D1EC540EE6D7E91F CRC64;
MLPPKIFFEK VKEIIWPIER KELKLFIPMA LMMLCILFNF GALRSIKDSL VVPSMGAEII
SFLKLWLVLP SCVIFTILYV KLSNKLNFEY IFYSIVGTFL LFFLLFAYII YPNQDIYHPN
DAMINNLIAS YPNLKWFIKI GSKWSYALMY IFSELWSAVV INLMFWQFAN HIFDTAKAKR
FYPVLGMVGN IGLIIAGSVL VFFSSGQYII DSELLTDSYN SSSNNSIMLQ PIISIIVTAG
IIAMFLFRII NKFILTNSIN VLDVKKVAAK TKTKLALIES IKLIIHSKYI GRIALLIICY
GLLINIVEGP WKAKIKELHP NTVDYVNFMG MFNIWMGISC VTFMIIGSNI LRRLGWLISA
LLTPIMLSIT GFMFFIFIIF IEEIGTCFGD FNLLYVAIIV GAIQNILSKS SKYSLFDSTK
EMAYIPLSLE LRTKGKAAVE VIGTKFGKSL GAFIQSLIFI IIPTATFDSI IIYLLVIFIV
MMNLWIWNII KLNKEYIKLC Q