TLCC_RICTY
ID TLCC_RICTY Reviewed; 501 AA.
AC Q68WQ3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=ADP,ATP carrier protein 3;
DE AltName: Full=ADP/ATP translocase 3;
GN Name=tlcC; Synonyms=tlc3; OrderedLocusNames=RT0464;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU03939.1; -; Genomic_DNA.
DR RefSeq; WP_011190922.1; NC_006142.1.
DR AlphaFoldDB; Q68WQ3; -.
DR STRING; 257363.RT0464; -.
DR EnsemblBacteria; AAU03939; AAU03939; RT0464.
DR KEGG; rty:RT0464; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; HPNTIDY; -.
DR OrthoDB; 427341at2; -.
DR Proteomes; UP000000604; 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..501
FT /note="ADP,ATP carrier protein 3"
FT /id="PRO_0000286474"
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; 57193 MW; 5145AEB78D2B2F23 CRC64;
MLPPKIFFEK FKEIIWPIER KELKLFIPMA LMMLCILFNF GALRSIKDSL VVPSMGAEII
SFLKLWLVLP SCVIFTVLYV KLSNKLNFEY IFYSIVGTFL LFFLLFAYII YPNQDIYHPN
DAMINNLIAS YPNLKWFIKI GSKWSYALMY IFSELWSAVV INLMFWQFAN HIFDTAKAKR
FYPVLGMIGN IGLIIAGSVL VFFSSGQYII DSELLTDSFN SSSCNSIILQ PIISIIVTAG
IIAMFLFRII NRFILTNAIN VLDVKKAAAR TKTKLALIES IKLIIHSKYI GRIALLIICY
GLLINIVEGP WKAKIKELHP NTIDYVNFMG MFNIWMGISC VTFMIIGSNI LRRLGWLISA
LLTPIMLSIT GFIFFIFIIF IEEIGTCFGD FNLLYVAIIV GAIQNILSKS SKYSLFDSTK
EMAYIPLSLE LRTKGKAAVE VIGTKFGKSL GAFIQSLIFI IIPTATFDSI IIYLLVIFIV
MMNLWIWNII KLNKEYIKLC K