CLPB2_SYNY3
ID CLPB2_SYNY3 Reviewed; 872 AA.
AC P74361;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Chaperone protein ClpB 2;
GN Name=clpB2; OrderedLocusNames=slr1641;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
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; BA000022; BAA18456.1; -; Genomic_DNA.
DR PIR; S76197; S76197.
DR AlphaFoldDB; P74361; -.
DR SMR; P74361; -.
DR IntAct; P74361; 6.
DR STRING; 1148.1653543; -.
DR PaxDb; P74361; -.
DR PRIDE; P74361; -.
DR EnsemblBacteria; BAA18456; BAA18456; BAA18456.
DR KEGG; syn:slr1641; -.
DR eggNOG; COG0542; Bacteria.
DR InParanoid; P74361; -.
DR OMA; SKMMQGE; -.
DR PhylomeDB; P74361; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; 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; IPR017730; Chaperonin_ClpB.
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 TIGRFAMs; TIGR03346; chaperone_ClpB; 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..872
FT /note="Chaperone protein ClpB 2"
FT /id="PRO_0000191193"
FT DOMAIN 6..148
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 9..73
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 85..148
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 161..342
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 343..551
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 561..772
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 773..872
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 393..527
FT /evidence="ECO:0000250"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 611..618
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 872 AA; 98123 MW; 7EAA8486C7D8D4D5 CRC64;
MQPTDPNKFT EKAWEAIAKT PEIAKQHRQQ QIETEHLLSA LLEQNGLATS IFNKAGASIP
RVNDQVNSFI AQQPKLSNPS ESIYLGRSLD KLLDNAEIAK SKYGDDYISI EHLMAAYGQD
DRLGKNLYRE IGLTENKLAE IIKQIRGTQK VTDQNPEGKY ESLEKYGRDL TELAREGKLD
PVIGRDEEVR RTIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIINHDV PESLRDRKLI
SLDMGALIAG AKYRGEFEER LKAVLKEVTD SQGQIILFID EIHTVVGAGA TQGAMDAGNL
LKPMLARGAL RCIGATTLDE YRKYIEKDAA LERRFQEVLV DEPNVLDTIS ILRGLKERYE
VHHGVKIADS ALVAAAMLSN RYISDRFLPD KAIDLVDEAA AKLKMEITSK PEELDEVDRK
ILQLEMERLS LQRENDSASK ERLEKLEKEL ADFKEEQSKL NGQWQSEKTV IDQIRTVKET
IDQVNLEIQQ AQRDYDYNKA AELQYGKLTD LQRQVEALET QLAEQQTSGK SLLREEVLES
DIAEIISKWT GIPISKLVES EKEKLLHLED ELHSRVIGQD EAVTAVAEAI QRSRAGLSDP
NRPTASFIFL GPTGVGKTEL AKALAKNLFD TEEALVRIDM SEYMEKHAVS RLMGAPPGYV
GYEEGGQLTE AIRRRPYSVI LFDEIEKAHG DVFNVMLQIL DDGRLTDAQG HVVDFKNTII
IMTSNLGSQY ILDVAGDDSR YEEMRSRVMD VMRENFRPEF LNRVDETIIF HGLQKSELRS
IVQIQIQSLA TRLEEQKLTL KLTDKALDFL AAVGYDPVYG ARPLKRAVQK YLETAIAKGI
LRGDYKPGET IVVDETDERL SFTSLRGDLV IV
