TLCD_RICBR
ID TLCD_RICBR Reviewed; 520 AA.
AC Q1RIG3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=ADP,ATP carrier protein 4;
DE AltName: Full=ADP/ATP translocase 4;
GN Name=tlcD; Synonyms=tlc4; OrderedLocusNames=RBE_0770;
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; ABE04851.1; -; Genomic_DNA.
DR RefSeq; WP_011477438.1; NC_007940.1.
DR AlphaFoldDB; Q1RIG3; -.
DR STRING; 336407.RBE_0770; -.
DR EnsemblBacteria; ABE04851; ABE04851; RBE_0770.
DR KEGG; rbe:RBE_0770; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; FLMTAIY; -.
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; Membrane; Nucleotide-binding; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..520
FT /note="ADP,ATP carrier protein 4"
FT /id="PRO_0000286484"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 520 AA; 58912 MW; 14FE3028AE0E71AB CRC64;
MTINQNNSNH TFSSHNLDNS PHKINKLINK FSDYIWPIKR QELSKFLFIT LLMFCILFIQ
NLIRALKDSI VTTMIGAETI SFLKFWGVMP CAFLMTAIYV KLVNRMKAEN IFYLIISIFL
AFFALFAYVI FPNHEILHLS PTTAQNLIAS LPNLKWFILL LSKWSFSLFY IIAELWPNVA
FALLFWQFVN NITTVEESKR FYPLFGLLSQ TGIYLAGQFL ENLSHINEYV VAKFSLQASF
HTLSVQIILT IVLILGIVGI KTFWLLNHKV LDKEHMALLR FKAKKKTMTI AESFQMILSS
RHIRLIATLL ICYGIAINLV EGPWKAAATK IYKTPTEYAA FIGNYLSYTG AFTILFVVLG
SNIVRKLGWF TAAIITPIIV FTTGILFFAV NNFESSAGLI VASFILTDPA LIAITIGAIQ
NVLSKSSKYT LFDSTKEMAY VPLDKEIKIK GKAAADVLGT KLGKSGSAFL QSLVFIILPS
ASYQSISVCL MFIFIITCLI WFWAVKELNK EYKKSVKFSQ