ID I4G5B3_MICAE Unreviewed; 886 AA.
AC I4G5B3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:CCI03124.1};
GN ORFNames=MICAC_4190012 {ECO:0000313|EMBL:CCI03124.1};
OS Microcystis aeruginosa PCC 9443.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Microcystaceae; Microcystis.
OX NCBI_TaxID=1160281 {ECO:0000313|EMBL:CCI03124.1, ECO:0000313|Proteomes:UP000003480};
RN [1] {ECO:0000313|EMBL:CCI03124.1, ECO:0000313|Proteomes:UP000003480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9443 {ECO:0000313|EMBL:CCI03124.1,
RC ECO:0000313|Proteomes:UP000003480};
RA Genoscope - CEA;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCI03124.1}.
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DR EMBL; CAIJ01000356; CCI03124.1; -; Genomic_DNA.
DR RefSeq; WP_002768913.1; NZ_HE972991.1.
DR AlphaFoldDB; I4G5B3; -.
DR HOGENOM; CLU_005070_4_1_3; -.
DR Proteomes; UP000003480; Unassembled WGS sequence.
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 78, MITOCHONDRIAL; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 6..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 415..531
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 855..886
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 886 AA; 100756 MW; 5E585A7424392C21 CRC64;
MQPTDSNKFT EQAWDSIVKS QEIARRFKNQ TLEVEHVIIA LLEQNNGLAT RILQKANIEI
PRLQQQLEVF TNRQPKVAIV DQLYLGRGLD LLLDRAEASR ESWQDKFISV EHLLVGFAED
ERVGRKCLRT FNLDPQDLEL AIKAIRGTQK VTEPNQEEKY EALDKYGRDL TAAAKEGKLD
PVIGRDEEIR RVVQVLSRRS KNNPVLIGEP GVGKTAIAEG LAQRIVNGDV PESLKNRQLI
SLDMGSLIAG AKYRGEFEER LRSVMKEVTQ SEGRIILFID ELHTVVGAGS REGGSMDAGN
LLKPMLARGE LRCIGATTLD EYRNHIEKDP PLERRFQQVY IKEPSVEDTI SILRGLKERY
ELHHGVTITD SALVAAATLS YRYISDRFLP DKAIDLVDEA AAKLEVESTT KPADLEMIDR
RLMQLRMEKF SLEKEEKKDR AFQERLERII EEIEELESKQ KPLADQWQTE KHIAEEIKLL
REEEEQLRLQ VEQAERAYDL NKAAQLKYGK LEILQGELEV KEKELETIQA AGSTLLRQQV
TDADIAEIVA RWTGIPVNRL MESERQKLLE LESHLQKKVV GQNEAVTAVA AAIRRARAGM
KDPSRPIGSF LFMGPTGVGK TELARALAGL LFDSEEAMVR IDMSEYMEKH AVSRLIGAPP
GYVGYEEGGQ LSEAVRRRPY SVVLLDEVEK AHRDVFNILL QVLDDGRITD SQGRVVDFRN
TIIVMTSNIG SDHILNVSED ADYEEMRKRV LTALRSHFRP EFLNRIDDLI IFHTLKKEEL
RYIVRLQLQR LERLLAEQKI NLELTTAAEN HIVTVGYDPT YGARPLKRAI QRELENPLAT
KILEQAFMEG DTVVIDCLDE VLSFSKKELE KEEQTLELAV VNLSSD
//
