TLC2_CHLMU
ID TLC2_CHLMU Reviewed; 543 AA.
AC Q9PJP6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=ADP,ATP carrier protein 2;
DE AltName: Full=ADP/ATP translocase 2;
GN Name=tlcB; OrderedLocusNames=TC_0782;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39585.1; -; Genomic_DNA.
DR PIR; F81665; F81665.
DR RefSeq; WP_010231516.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PJP6; -.
DR STRING; 243161.TC_0782; -.
DR EnsemblBacteria; AAF39585; AAF39585; TC_0782.
DR GeneID; 1246147; -.
DR KEGG; cmu:TC_0782; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_0; -.
DR OMA; ICAGEIS; -.
DR OrthoDB; 427341at2; -.
DR Proteomes; UP000000800; 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..543
FT /note="ADP,ATP carrier protein 2"
FT /id="PRO_0000102588"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
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 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..497
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 510..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 543 AA; 59672 MW; 6291A671F1924D7D CRC64;
MSSEVKTFSK FRRYFFPIHK SEFPKFIPLL LLAFFVGFNY SLLKTTKDSL VLAGSRAGAE
VIPFLKVWGI VPGAVIITMI YGWMSCRYSR GFVFCALVGG FLSFFALFAC VIYPMGDALH
LNGLAAKLQT ILPRGARGFV VMVQYWSYSL YYVMSELWSS VVLSTLFWGI ANHITSVREA
GRFYALINVG LNVSSIVAGE ISLWLGKHTL IPSSMAVDAW HGVLLNITLL IVAAGGLILY
LYRKLDHLTE EAPVLGDGLV SEMSVAQLKQ EKKRPKAKAK SLLSVLFRSR YLMGIAVVVL
AYNLAIHLLE VVWKEQVCQI YSSRVEFNSY MSRITAFTGI VSALAGVFAA GQSIRRWGWT
VGALITPLTM LITGGLFFGA IYAVKGDAMI LGGFLGFSPL VLTAWLGGVQ NVFSRAIKFT
YFDQTKEMAF IPLEDDEKDY GKAAIDGVIS RVGKSGGSLV YQALLIIFSS VADCMNAITI
VLLLALGGWI WVVAWLGKEY SVRTAALGKA RAAEEPSLQD EDESRVSSPI SEPEAREEVV
TTL