CLPX_CHLTB
ID CLPX_CHLTB Reviewed; 419 AA.
AC B0BAG0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000255|HAMAP-Rule:MF_00175};
GN Name=clpX {ECO:0000255|HAMAP-Rule:MF_00175}; OrderedLocusNames=CTLon_0074;
OS Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471473;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCH-1/proctitis;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC directs the protease to specific substrates. Can perform chaperone
CC functions in the absence of ClpP. {ECO:0000255|HAMAP-Rule:MF_00175}.
CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC into a disk-like structure with a central cavity, resembling the
CC structure of eukaryotic proteasomes. {ECO:0000255|HAMAP-Rule:MF_00175}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000255|HAMAP-
CC Rule:MF_00175}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM884177; CAP06472.1; -; Genomic_DNA.
DR RefSeq; WP_009873309.1; NC_010280.2.
DR AlphaFoldDB; B0BAG0; -.
DR SMR; B0BAG0; -.
DR KEGG; ctl:CTLon_0074; -.
DR HOGENOM; CLU_014218_8_2_0; -.
DR OMA; HYKRVQA; -.
DR Proteomes; UP000000794; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 6.20.220.10; -; 1.
DR HAMAP; MF_00175; ClpX; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR046425; ClpX_bact.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR Pfam; PF06689; zf-C4_ClpX; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SMART; SM00994; zf-C4_ClpX; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00382; clpX; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Metal-binding; Nucleotide-binding; Zinc.
FT CHAIN 1..419
FT /note="ATP-dependent Clp protease ATP-binding subunit ClpX"
FT /id="PRO_1000097937"
FT DOMAIN 1..50
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01250"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00175"
SQ SEQUENCE 419 AA; 46183 MW; C52CCCB03DA63772 CRC64;
MTKKNLAVCS FCGRSEKDVE KLIAGPSVYI CDYCIKLCSG ILDKTPAPAT QEIATSSTSS
PTSLRVLTPK EIKRHIDSYV IGQERAKKTI SVAVYNHYKR IRALMQDKQV SYGKSNVLLL
GPTGSGKTLI AKTLAKILDV PFTIADATTL TEAGYVGEDV ENIVLRLLQA ADYDVARAER
GIIYIDEIDK IGRTTANVSI TRDVSGEGVQ QALLKIIEGT VANIPPKGGR KHPNQEYIRV
NTENILFIVG GAFVNLDKII AKRLGRTTIG FSEETDLAVT NRDHLLAKVE TEDLITFGMI
PEFIGRFNCI VNCEELTLDE LVEILTEPAN AIVKQYTELF EEENVKLIFE KEALYAIAQK
AKQAKTGARA LGMILENLLR DLMFEIPSDP TVEAIRIEED TITQNKPPVI IQKSPEAIA