TLCB_RICBR
ID TLCB_RICBR Reviewed; 507 AA.
AC Q1RHU3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ADP,ATP carrier protein 2;
DE AltName: Full=ADP/ATP translocase 2;
GN Name=tlcB; Synonyms=tlc2; OrderedLocusNames=RBE_0990;
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; ABE05071.1; -; Genomic_DNA.
DR RefSeq; WP_011477651.1; NC_007940.1.
DR AlphaFoldDB; Q1RHU3; -.
DR STRING; 336407.RBE_0990; -.
DR EnsemblBacteria; ABE05071; ABE05071; RBE_0990.
DR KEGG; rbe:RBE_0990; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_5; -.
DR OMA; HIVWPIR; -.
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..507
FT /note="ADP,ATP carrier protein 2"
FT /id="PRO_0000286482"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 507 AA; 58624 MW; 8EE461ED6506D2CC CRC64;
MDAVNSNFTF WNRARNSKFR HIVWPIRSYE LTKFIPMALL MFFILLNQNL VRSIKDSFVV
TLINTEVLSF IKLWGEMPMG VLFVILYSKL CNLMTTEQVF RIITSTFLLF FAFFGFVLFP
YREFFHPDPE LVKHYITVLP HLKWFIIIWG QWSLVLFYIM GELWPVIVFT LLYWQLANKI
TKVEEAPRFY SFFTLFGQTN LLISGTIIIY FAKSEHFLLP LFSHLSDTNE ILLKSFVSII
LVSGLICLAL HKFIDKTVVE SDKNIKFKNQ RTDILKLSLI ESTKIILTSR YLGFICILLI
SYSMSISLIE GLWMSKVKQL YPDTKDFISY HGKVFFWTGV LTLVSAFLGS NLIRLCGWFW
GAIITPIMMF GAGVMFFSFT VFENHLKNII DTLGYSSPLI VIVFIGGLWH VLSKSVKYSL
FDATKEMVYI PLDSEMKTKG KAAVDVMGTK IGKSIGAIIQ FISFSIFPNA VHNDIAGLLM
FSFIIVCLIW LYGVKVLAEY YNKLVKR