TLCC_RICBR
ID TLCC_RICBR Reviewed; 504 AA.
AC Q1RIL2;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=ADP,ATP carrier protein 3;
DE AltName: Full=ADP/ATP translocase 3;
GN Name=tlcC; Synonyms=tlc3; OrderedLocusNames=RBE_0721;
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; ABE04802.1; -; Genomic_DNA.
DR RefSeq; WP_011477389.1; NC_007940.1.
DR AlphaFoldDB; Q1RIL2; -.
DR STRING; 336407.RBE_0721; -.
DR EnsemblBacteria; ABE04802; ABE04802; RBE_0721.
DR KEGG; rbe:RBE_0721; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; HPNTIDY; -.
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..504
FT /note="ADP,ATP carrier protein 3"
FT /id="PRO_0000286483"
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 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 504 AA; 57380 MW; 862F265EAD921B0E CRC64;
MLPPKTFFEK VKEIIWPIER KELKLFIPMA LMMLCILFNF GALRSIKDSL VVPSMGAEII
SFLKLWLVLP ACVIFTILYV KLSNKFNFEY VFYIIVGSFL LFFLFFAYII YPNQEAYHPN
NEIINSLITS YPNFKWFIKI ASKWSYGLMY IFAELWSAVV INLMFWQFAN HIFDTNKAKR
FYPVLGMVGN IGLILAGSVL VFFSGNKIID PELLPNSFDA SVNLTSQTTE MLQPIMSIIV
AAGVISMLLF RIINKSILTD SINVLDSKKV KAKTKTKLSV LESIKLVINS KYIGRIALLI
ICYGLLINIV EGPWKAKVKE LYPSTIDYVH FMGRFNILMG ISCVTFMIIG SNILRRLGWF
FSALLTPIML SITGLMFFIF IIFIEEIGSC FGNFNLLYAA IIVGAIQNIL SKSSKYSLFD
STKEMAYIPL SLELRTKGKA AVEVIGTKFG KSLGAFIQSL IFIIIPTATF DSIIIYLLVI
FIVMISLWIW DVVKLNKEYT ELCK