ID   CLPC_CHLMU              Reviewed;         870 AA.
AC   Q9PKA8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Probable ATP-dependent Clp protease ATP-binding subunit;
GN   Name=clpC; OrderedLocusNames=TC_0559;
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   -!- SIMILARITY: Belongs to the ClpA/ClpB family. ClpC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE002160; AAF39398.1; -; Genomic_DNA.
DR   PIR; B81689; B81689.
DR   AlphaFoldDB; Q9PKA8; -.
DR   SMR; Q9PKA8; -.
DR   STRING; 243161.TC_0559; -.
DR   PRIDE; Q9PKA8; -.
DR   EnsemblBacteria; AAF39398; AAF39398; TC_0559.
DR   KEGG; cmu:TC_0559; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_0; -.
DR   OMA; ERMKAVM; -.
DR   Proteomes; UP000000800; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Repeat.
FT   CHAIN           1..870
FT                   /note="Probable ATP-dependent Clp protease ATP-binding
FT                   subunit"
FT                   /id="PRO_0000191230"
FT   DOMAIN          18..161
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   DOMAIN          460..495
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00217"
FT   REGION          21..86
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          97..161
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          167..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..192
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         251..258
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         588..595
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   870 AA;  97008 MW;  F0E11C69C379CD3C CRC64;
     MSYMLKSIPP RHIQVFMFEK FTNRAKQVIK LAKKEAQRLN HNYLGTEHIL LGLLKLGQGV
     AVNVLRTLGV DFDTAKNEVE RLIGYGPEIQ VYGDPALTGR VKKSFESANE EASILEHNYV
     GTEHLLLGIL NQADGVALQV LENLHIDPKE IRKEILKELE TFNLQLPPSS SITPRNTNSS
     SSSSSKSSSL GGHSLGGDKP EKLSALKAYG YDLTEMFKEA RLDPVIGRSA EVERLILILC
     RRRKNNPVLI GEAGVGKTAI VEGLAQKIVS GEVPEALRKK RLITLDLALM IAGTKYRGQF
     EERIKAVMDE VRKHGNILLF IDELHTIVGA GAAEGAIDAS HILKPALARG EIQCIGATTL
     DEYRKHIEKD AALERRFQKI VVQPPSVDET VEILRGLKKK YEEHHNVFIT DEALVAAAKL
     SDQYVHGRFL PDKAIDLLDE AGARVRVNTM GQPSELLRLE AEIESTKQAK EQAIGTQEYE
     KAASLRDEEK KLREKLSNMK QQWESNKEEH QVPVDEEAVA QVVSVQTGIP AARLTEAESE
     KLLMLENTLQ KKVIGQDQAV ASICRAIRRS RTGIKDPNRP MGSFLFLGPT GVGKTLLAQQ
     IAVEMFGGED SLIQVDMSEY MEKFAATKMM GSPPGYVGHE EGGHLTEQVR RRPYCVVLFD
     EIEKAHPDIM DLMLQILEQG RLTDSFGRKI DFRNTIIIMT SNLGADLIRK TGEIGFGLRS
     HMDYGVIKEK IDAAVKKHLK PEFINRLDES VIFKPLEKEA LSEIIHLEIN KLGSRLQNHQ
     MALNIPDSVV SFLVDKGHSP EMGARPLRRV VEQYLEDPLA EMLLKESCRQ EARKLCARLI
     EERVIFERED EISALAVEGD GPASVTADES