CLPB_PARUW
ID CLPB_PARUW Reviewed; 868 AA.
AC Q6MD97;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Chaperone protein ClpB;
GN Name=clpB; OrderedLocusNames=pc0728;
OS Protochlamydia amoebophila (strain UWE25).
OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC Candidatus Protochlamydia.
OX NCBI_TaxID=264201;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWE25;
RX PubMed=15073324; DOI=10.1126/science.1096330;
RA Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA Mewes H.-W., Wagner M.;
RT "Illuminating the evolutionary history of chlamydiae.";
RL Science 304:728-730(2004).
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}.
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DR EMBL; BX908798; CAF23452.1; -; Genomic_DNA.
DR RefSeq; WP_011175278.1; NC_005861.1.
DR AlphaFoldDB; Q6MD97; -.
DR SMR; Q6MD97; -.
DR STRING; 264201.pc0728; -.
DR PRIDE; Q6MD97; -.
DR EnsemblBacteria; CAF23452; CAF23452; PC_RS03505.
DR KEGG; pcu:PC_RS03505; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_0; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 44062at2; -.
DR Proteomes; UP000000529; 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;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..868
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000191151"
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 5..70
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 82..146
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 159..340
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 341..546
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 556..770
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 771..868
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 391..525
FT /evidence="ECO:0000250"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 606..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 868 AA; 98546 MW; 916F3BBEA2CC53C9 CRC64;
MNQNFTDHVA EAIQAAFAEA QRLNHTEVTE NHLLWAFLKD KEGYFYSLLN GLGTNPQKLF
QETENNIHHL PTYSGGGQAP NPSRSLQSRI VDAQNIAQSW KDTYTSSDHF LISYWKNGGD
PFASWKKKTT ISLEKLEEQI KKIRGDRHMD SPSSESNLQA LEKYCKNLTD LARQGKLDPV
IGRDEEIRRT MQVLCRRTKN NPMLIGDPGV GKTAIAEGLA QRIVQQDIPD SLKNKQLLAL
DMGSLIAGTK YRGEFEERLK GILQDIEKSE GQIILFIDEV HTLIGAGATD GAMDAANLLK
PALARGILHC IGATTLNEYQ KYIEKDAALE RRFQLVLVNE PTIEDSIAIL RGLRERYEIY
HGVHITESAI HAAVLLSSRY ITDRRLPDKA IDLIDESASL IRMQLGSRPL PIDNKERELA
GLIVEQEAMK RESTPLAKNE VEKLEGRIAQ IKEELKILRE QWDQEKKIIE SLKEKKDKLE
KLRFEEEAAE RKADYNRVAE LRYNLIPQLQ KEIEEAQTQL NNKPNRLLQE EVDESLIAQI
VSKWTGIPVH KMLEGEAERL LHLENELEKR VVGQEIAVSA VSEAIRRSRS GLSDPNRPMG
VFLFLGPTGV GKTELAKALA FQLFNQDEAL IRLDMSEYME KHTVSKLIGS PPGYIGYEEG
GQLTEALRRR PYAVVLFDEI EKAHPDVFNI LLQVFDDGRL TDSKGRVVNC KNALFIMTSN
IGSDLLLEKM EQNKQGLAKD EIMLVLDPVI KKHFRPEFIN RLDDILPFVP LREHDMEKIV
VIQLNLLAKR LKDRDVELMW TPQALAHLAK EGYDPHFGAR PLKRYIQQEV INQLSTAILE
GKIPPHSHIK LELEGNTIRF KSFAGGKN
