ID E0U8Y4_GLOV7 Unreviewed; 872 AA.
AC E0U8Y4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 85.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN OrderedLocusNames=Cyan7822_4205 {ECO:0000313|EMBL:ADN16123.1};
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:ADN16123.1, 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; ADN16123.1; -; Genomic_DNA.
DR RefSeq; WP_013324186.1; NC_014501.1.
DR AlphaFoldDB; E0U8Y4; -.
DR STRING; 497965.Cyan7822_4205; -.
DR KEGG; cyj:Cyan7822_4205; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_3; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 9803641at2; -.
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..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 779..806
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 99059 MW; C1349E11B600E5A2 CRC64;
MQPTNPNQFT EKAWEAIVKT PDIAKQNKQQ QIESEHLMKS LLEQEGLASS IFNKANVSVQ
RLRDKTDEFI RRQPTLSNPS ESVYLGRSLD SLLDRAEGFR KEFGDDFISI EHLILAYAKD
DRFGRALFQE FGLSENKLKD IIKQVRGTQK VTDQNPEGKY EALEKYGRDL TQLAREGKLD
PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIVEG LAQRIINRDV PESLRDRKLI
ALDLGGLIAG AKYRGEFEER LKAVLKEVTD SQGNIIMFID EIHTVVGAGA TQGAMDASNL
LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQSVYV DEPNVVDTIS ILRGLKERYE
VHHGVKIADT ALVAAAVLSN RYISDRFLPD KAIDLVDEAA AKLKMEITSK PEELDEVDRK
ILQLEMERLS LQKEDDPLSR ERLGRLEKEL ADLKEEQTQY NAQWQAEKEL IDKLRTVKKE
IEQVNVEIQQ AERDYDYNKA AELRYGKLTD LQRQIKELES QITDKQTSGK TLLREEVVES
DIAEIISKWT GIPISKLVES EKEKLLHLED ELHQKVVGQD EAVTAVADAI QRSRAGLADP
NRPTASFIFL GPTGVGKTEL AKALALNLFD SEEALVRIDM SEYMEKHAVS RLLGAPPGYV
GYEEGGQLTE AIRRRPYSVI LFDEIEKAHN DVFNVMLQIL DDGRLTDSQG RTVDFKNTII
IMTSNIGSQV ILDIAGDDSR YDEMRSRVME AMRNSFRPEF LNRVDEIIIF HSLQKSQLRE
IVKLQVKRLE DRLSEQKLSL KLSEQALDYL ADIGYDPVYG ARPLKRAVQR YLETAIAKAI
LRGDFKQGDM IFVDVTDERL TFTRLPAEVL TT
//