ID   Y697_CHLMU              Reviewed;         236 AA.
AC   Q9PJX9;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Probable metal transport system ATP-binding protein TC_0697;
GN   OrderedLocusNames=TC_0697;
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   -!- FUNCTION: Part of an ATP-driven transport system
CC       TC_0696/TC_0697/TC_0698 for a metal. Probably responsible for energy
CC       coupling to the transport system.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE002160; AAF73593.1; -; Genomic_DNA.
DR   RefSeq; WP_010231251.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PJX9; -.
DR   SMR; Q9PJX9; -.
DR   STRING; 243161.TC_0697; -.
DR   EnsemblBacteria; AAF73593; AAF73593; TC_0697.
DR   GeneID; 1246059; -.
DR   KEGG; cmu:TC_0697; -.
DR   eggNOG; COG1121; Bacteria.
DR   HOGENOM; CLU_000604_1_11_0; -.
DR   OMA; GHDHVHP; -.
DR   OrthoDB; 1721927at2; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Transport.
FT   CHAIN           1..236
FT                   /note="Probable metal transport system ATP-binding protein
FT                   TC_0697"
FT                   /id="PRO_0000093232"
FT   DOMAIN          5..236
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   236 AA;  26329 MW;  CEC9EB0C82E95026 CRC64;
     MTKQLILENV SFRYGKTGPW IVDHVSCEVH SGDFIGIIGP NGGGKTTLTQ LMLGLLQPVC
     GKIFTCFTQE NRPLSIGWVP QHFAYDAAFP ITVKETVLSG RLATLPWYGR YTKKDHDAAE
     EALHTVDLLE YKDSCFSHLS GGQIQRVLLA RALSARPKFL LLDEPTANID PSNQQKILQI
     LSDLNKHCTI LMITHDLHHT AGCFNRVFFM NKKLTALADT TTISERFCCN TFGKCS