TLC1_CHLMU
ID TLC1_CHLMU Reviewed; 529 AA.
AC Q9PKX5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=ADP,ATP carrier protein 1;
DE AltName: Full=ADP/ATP translocase 1;
GN Name=tlcA; OrderedLocusNames=TC_0335;
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; AAF39198.1; -; Genomic_DNA.
DR PIR; C81714; C81714.
DR RefSeq; WP_010230191.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PKX5; -.
DR STRING; 243161.TC_0335; -.
DR EnsemblBacteria; AAF39198; AAF39198; TC_0335.
DR GeneID; 1246379; -.
DR KEGG; cmu:TC_0335; -.
DR eggNOG; COG3202; Bacteria.
DR HOGENOM; CLU_023964_0_1_0; -.
DR OMA; RKVIWPI; -.
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..529
FT /note="ADP,ATP carrier protein 1"
FT /id="PRO_0000102585"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 509..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 529 AA; 58304 MW; EED13A4C751071C9 CRC64;
MTQTAEKPFG KLRSFLWPIH MHELKKVLPM FLMFFCISFN YTILRDTKDT LIVTAPGSGA
EAIPFIKLWL VVPSAVVFML IYAKLSNILS KQALFYAVLS PFVVFFALFP LVIYPYRHIL
HPTDFADTLQ AILPSGFLGF IAMLRNWTFA AFYVLSELWG SVMLSLMFWG FANEITKISE
AKRFYALFGV GANVALLISG PAIVWSSKLR ASLGEGVDPW GVTLYFLMAM FLCSCAIIAA
CYWWMNRYVL TDPRFYNPAE LKAKKSKPKM SMGESFSYLL RSPYMLLLAL LVICYGVCIN
LVEVTWKSQL KMQFPNPNEY SAFMGTFSFW TGVVSVFVML FIGGNVIRRF GWLTGALVTP
VMVLVTGAIF FALVIFRDHA TGLVAALGTT PLMLAVVVGA VQNILSKSTK YALFDATKEM
AYIPLDQEQK VKGKAAIDVV AARFGKSGGS LIQQGLLVVC GSISAMTPFL AVALFAIIMV
WLTSATKLNK LFLAASAAKE QELAEATAAA EKEASPAAKE VSPAIEGVS