CLPB1_SYNY3
ID CLPB1_SYNY3 Reviewed; 898 AA.
AC P74459;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Chaperone protein ClpB 1;
GN Name=clpB1; OrderedLocusNames=slr0156;
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; BAA18560.1; -; Genomic_DNA.
DR PIR; S76431; S76431.
DR AlphaFoldDB; P74459; -.
DR SMR; P74459; -.
DR DIP; DIP-48813N; -.
DR IntAct; P74459; 3.
DR STRING; 1148.1653648; -.
DR PaxDb; P74459; -.
DR EnsemblBacteria; BAA18560; BAA18560; BAA18560.
DR KEGG; syn:slr0156; -.
DR eggNOG; COG0542; Bacteria.
DR InParanoid; P74459; -.
DR OMA; GPEHILM; -.
DR PhylomeDB; P74459; -.
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..898
FT /note="Chaperone protein ClpB 1"
FT /id="PRO_0000191192"
FT DOMAIN 6..148
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 9..74
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..344
FT /note="NBD1"
FT /evidence="ECO:0000250"
FT REGION 345..560
FT /note="Linker"
FT /evidence="ECO:0000250"
FT REGION 570..781
FT /note="NBD2"
FT /evidence="ECO:0000250"
FT REGION 782..898
FT /note="C-terminal"
FT /evidence="ECO:0000250"
FT COILED 395..536
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 620..627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 898 AA; 101392 MW; 67BBA62136E36D63 CRC64;
MQPTDPTKFT EQAWDAIVKS QEVARRYKNT NLEVEHILLA LLEQDMGLAA RIFQRAAVDG
EGLRQQLEIF TNRQPKQAYV EQLYLGRSLD VMLDRADAAR SSWEDKFISV EHLLVGFAED
DRVGRKTLRA FNLDPQDLEL AIKAIRGSQK VTEPNQEEKY EALDKYGRDL TEQARQGKLD
PVIGRDEEIR RVIQVLSRRS KNNPVLIGEP GVGKTAIAEG LAQRIINGDV PESLKNRQLI
SLDMGSLIAG AKYRGEFEER LRSVMKEVTN SDGQIILFID EVHTVVGAGG REGSGSMDAG
NLLKPMLARG ELRCIGATTL DEYRKNIEKD PALERRFQQV YVKQPSVDDT ISILRGLKEK
YEVHHGVKIT DSALVAAATL SHRYIQDRFL PDKAIDLVDE AAARLKMEIT SKPVELEDID
RRLMQLQMEK LSLEGEEKRP GLGADKSSKE RLEKIQQEIT ELEGQQQELS GQWLSEKQML
EEINTLKEKE QELRLQVEKA ERATDWEKAA KIKYGELEVL QHDIEEKESK LLEIQGSGNT
LLREQVTESD IAEIVAGWTG IPMNRLMETE RQKLLQLEGH LHQRVIGQKE AVAAVSAAIR
RARAGMKDPS RPIGSFLFMG PTGVGKTELA RALAGFLFDS EEAMVRIDMS EYMEKHAVSR
LIGAPPGYVG YEEGGQLSEA VRRRPYSVVL LDEVEKAHLD VFNILLQVLD DGRITDSQGR
VVDFRNTIIV MTSNIGSDHI LSLSADDADY DKMQKQVLQS LRKHFRPEFL NRIDDLIIFH
TLKRDELRRI VVLQIKRIEK LLDEQKITLS LSDAALDHIV SAGYDPTYGA RPLKRAIQRQ
LENPIATKIL ENTFVAGDKI LIDCVDGQLI FDKEIEPTTL PEEPEENITA VEVEVLSS
