TLC2_CHLTR
ID TLC2_CHLTR Reviewed; 540 AA.
AC O84502;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=ADP,ATP carrier protein 2;
DE AltName: Full=ADP/ATP translocase 2;
GN Name=tlcB; OrderedLocusNames=CT_495;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ADP/ATP translocase tlc family.
CC {ECO:0000305}.
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DR EMBL; AE001273; AAC68096.1; -; Genomic_DNA.
DR PIR; E71503; E71503.
DR RefSeq; NP_220009.1; NC_000117.1.
DR RefSeq; WP_009871857.1; NC_000117.1.
DR AlphaFoldDB; O84502; -.
DR STRING; 813.O172_02725; -.
DR PRIDE; O84502; -.
DR EnsemblBacteria; AAC68096; AAC68096; CT_495.
DR GeneID; 884269; -.
DR KEGG; ctr:CT_495; -.
DR PATRIC; fig|272561.5.peg.538; -.
DR HOGENOM; CLU_023964_0_1_0; -.
DR InParanoid; O84502; -.
DR OMA; ICAGEIS; -.
DR Proteomes; UP000000431; 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..540
FT /note="ADP,ATP carrier protein 2"
FT /id="PRO_0000102590"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 540 AA; 59764 MW; 126398B58C4A17AB CRC64;
MSSEVKSFSK FRGYFFPIYR SEFSKFIPLF FLAFFVGVNY ALLKTTKDSL VLVGSRAGAE
VIPFLKVWGI VPGAVIVTMI YGWMSRRYSR GTVFISLVGG FLGFFALFAT VIYPIGDALH
LNKLAAKLQS ILPPGGRGFV VMVQYWSYSL YYVMSELWSS IVLSTLFWGV ANHITSVREA
GRFYALINTG LNLSSVFAGE VSLWLGRNPV IAFPMAVDPW HEVLLNITLL IVLAGGVILY
LYQKLDRLMD ETSMLKEGLA AEMSVAQLKK EKKRSKAKAK SLFALLLRSR YLLGIAVVVL
SYNLVIHLFE VVWKDQVCRI YASRVEFNSY MSRITTLTGI VSALTGIFAA GQTIRRWGWT
IGALVPPLTM LITGALFFGA IYAVKGDAMI FGGILGISPL VLTAWLGGVQ NVFSRAIKFT
YFDQTKEMAF IPLEDDEKNY GKAAIDGVIS RVGKSGGSLV YQGLLIIFSS VAASLNAITI
VLLLALGSWI FVIAWLGREY TAKTEALFRV NVSEEDVLQE EREASSLVDA ESREEPVTTL
