CLPB_CHLPN
ID CLPB_CHLPN Reviewed; 866 AA.
AC Q7AJA9; Q7VQ76; Q9K226; Q9Z939;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=CPn_0144, CP_0629, CpB0145;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC discriminating domain, recruiting aggregated proteins to the ClpB
CC hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC hexamer probably in an ATP-dependent manner. The movement of the
CC coiled-coil domain is essential for ClpB ability to rescue proteins
CC from an aggregated state, probably by pulling apart large aggregated
CC proteins, which are bound between the coiled-coils motifs of adjacent
CC ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF38444.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP98078.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE001363; AAD18297.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38444.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000008; BAA98354.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98078.1; ALT_INIT; Genomic_DNA.
DR PIR; E72113; E72113.
DR PIR; H81556; H81556.
DR PIR; H86508; H86508.
DR RefSeq; NP_224352.1; NC_000922.1.
DR RefSeq; WP_010882794.1; NZ_LN847257.1.
DR AlphaFoldDB; Q7AJA9; -.
DR SMR; Q7AJA9; -.
DR STRING; 115711.CP_0629; -.
DR EnsemblBacteria; AAD18297; AAD18297; CPn_0144.
DR EnsemblBacteria; AAF38444; AAF38444; CP_0629.
DR GeneID; 45050189; -.
DR KEGG; cpa:CP_0629; -.
DR KEGG; cpj:clpB; -.
DR KEGG; cpn:CPn_0144; -.
DR KEGG; cpt:CpB0145; -.
DR PATRIC; fig|115713.3.peg.162; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; -; 3.
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; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
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; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding; Repeat;
KW Stress response.
FT CHAIN 1..866
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191106"
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 4..69
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 81..145
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 158..339
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 340..545
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 555..769
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 770..866
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 390..524
FT /evidence="ECO:0000250"
FT BINDING 205..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 605..612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 866 AA; 96928 MW; F50CA051756A9323 CRC64;
MEKFSDAVSE ALEKAFELAK SSKHTYVTEN HLLLALLENT ESLFYLVIKD IHGNPGLLNT
AVKDALSREP TVVEGEVDPK PSPGLQTLLR DAKQEAKTLG DEYISGDHLL LAFWSSNKEP
FNSWKQTTKV SFKDLKNLIT KIRRGNRMDS PSAESNFQGL EKYCKNLTAL AREGKLDPVI
GRDEEIRRTI QVLSRRTKNN PMLIGEPGVG KTAIAEGLAL RLIQGDVPES LKGKQLYVLD
MGALIAGAKY RGEFEERLKS VLKDVESGDG EHIIFIDEVH TLVGAGATDG AMDAANLLKP
ALARGTLHCI GATTLNEYQK YIEKDAALER RFQPIFVTEP SLEDAVFILR GLREKYEIFH
GVRITEGALN AAVLLSYRYI PDRFLPDKAI DLIDEAASLI RMQIGSLPLP IDEKERELAA
LIVKQEAIKR EQSPSYQEEA DAMQKSIDAL REELASLRLG WDEEKKLISG LKEKKNSLES
MKFSEEEAER VADYNRVAEL RYSLIPQLEE EIKQDEASLN QRDNRLLQEE VDERLIAQVV
ANWTGIPVQK MLEGEAEKLL ILEESLEERV VGQPFAVSAV SDSIRAARVG LNDPQRPLGV
FLFLGPTGVG KTELAKALAD LLFNKEEAMV RFDMSEYMEK HSISKLIGSS PGYVGYEEGG
SLSEALRRRP YSVVLFDEIE KADKEVLNIL LQVFDDGILT DGKKRKVNCK NALFIMTSNI
GSPELADYCS KKGSELTKEA ILSVVSPVLK RYLSPEFMNR IDEILPFVPL TKEDIVKIVG
IQMRRIAQRL KARRINLSWD DSVILFLSEQ GYDSAFGARP LKRLIQQKVV ILLSKALLKG
DIKPDTSIEL TMAKEVLVFK KVETPS
