ID E0UHA4_GLOV7 Unreviewed; 924 AA.
AC E0UHA4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Cyan7822_4927 {ECO:0000313|EMBL:ADN16818.1};
OS Gloeothece verrucosa (strain PCC 7822) (Cyanothece sp. (strain PCC 7822)).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Aphanothecaceae; Gloeothece; Gloeothece verrucosa.
OX NCBI_TaxID=497965 {ECO:0000313|EMBL:ADN16818.1, ECO:0000313|Proteomes:UP000008206};
RN [1] {ECO:0000313|Proteomes:UP000008206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7822 {ECO:0000313|Proteomes:UP000008206};
RX PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA Sherman L.A., Pakrasi H.B.;
RT "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT unicellular nitrogen-fixing Cyanobacteria.";
RL MBio 2:E214-E214(2011).
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. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP002198; ADN16818.1; -; Genomic_DNA.
DR AlphaFoldDB; E0UHA4; -.
DR STRING; 497965.Cyan7822_4927; -.
DR KEGG; cyj:Cyan7822_4927; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_3; -.
DR OMA; GPEHILM; -.
DR Proteomes; UP000008206; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
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; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000008206};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 6..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 444..536
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 924 AA; 105343 MW; 7A0FC0719C794369 CRC64;
MQPTDSSKFT EQAWDAIVKS QEVARRYKNQ TLEVEHVVIA LLEQEKGLAT RIFNRAEIDQ
IRLKQQLETF ASRQPKIPSV ELYLGRGLDI MLDRAEASRE SWQDKFISVE HLLVGFAEDE
RIGRRCLRSF NLDPQDLEAH IKAIRGTQKV TEANQEERYE ALAKYGRDLT EQAKEGKLDP
VIGRDEEIRR VVQVLSRRSK NNPVLIGEPG VGKTAIAEGL AQRIVNKDVP ESLKNRQLIS
LDMGSLIAGA KYRGEFEERL RTVMKEVTQS DGQIILFIDE LHTVVGAGSR EGGSMDAGNL
LKPMLARGEL RCIGASTLDE YRKHIEKDPA LERRFQQVYI KEPSVEDTIS ILRGLKERYE
VHHGVKITDS ALVAAATLSH RYITDRFLPD KAIDLVDEAA AKLKMEITSK PTELESIDRR
LMQLEMEKLS LAGEEKRPGI TVLDRAYKER LDRIEQEIQE LKVQQQDLSS QWQGEKQLLD
EIKGLKEEEE QLRLQVEQAE RAYDLNKAAQ LKYGKLQVLQ QEIEAKEIKL LELQAEGTCL
LREQVSEADI AEIVARWTGI PINRLLETER QKLLQLEHHL HERVIGQTEA VAAVAAAIRR
ARAGMKDPSR PIGSFLFMGP TGVGKTELAR ALAQFLFDSE EAMVRIDMSE YMEKHAVSRL
IGAPPGYVGY EEGGQLSEAV RRRPYSVVLL DEVEKAHRDV FNILLQVLDD GRITDSQGRV
VDFRNTIIVM TSNIGSEHIL NVSANDTDYE EMRKRVLVAL RKHFRPEFLN RIDDLIIFHT
LKKDELRHIV RLQLQRIQRL LSEQKISLDL TNAAQDYIVN VGYDPTYGAR PLKRAIQREL
ENPLAMKILE QSFIEGDTVV IDCVDNALTF NKDQVQDHVQ DHVQVQAQDH VQDHVQVQAQ
LEDDDDDDDD DEVIETVVPE IVYP
//