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Database: UniProt
Entry: E0UHA4_GLOV7
LinkDB: E0UHA4_GLOV7
Original site: E0UHA4_GLOV7 
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
//
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