ID A0A1Z4JFG7_LEPBY Unreviewed; 895 AA.
AC A0A1Z4JFG7;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=NIES2135_23040 {ECO:0000313|EMBL:BAY55481.1};
OS Leptolyngbya boryana NIES-2135.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1973484 {ECO:0000313|EMBL:BAY55481.1, ECO:0000313|Proteomes:UP000217895};
RN [1] {ECO:0000313|EMBL:BAY55481.1, ECO:0000313|Proteomes:UP000217895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2135 {ECO:0000313|EMBL:BAY55481.1,
RC ECO:0000313|Proteomes:UP000217895};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) 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}.
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DR EMBL; AP018203; BAY55481.1; -; Genomic_DNA.
DR RefSeq; WP_017287040.1; NZ_AP018203.1.
DR AlphaFoldDB; A0A1Z4JFG7; -.
DR Proteomes; UP000217895; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000217895};
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..537
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 895 AA; 100612 MW; 621E9DB3FD382C9D CRC64;
MQPTDPSKFT DKAWEAIVQA QDVVRRYRHQ NLEVEHLMIS LLEQEDGLAA KILTKVGVEA
TRLWQQIDEY ARRQPKVGSS EQLYLGRNLD VMLDRAETAR VAMQDDFISI EHLLKSFADD
PRLGMKLFRS LNVDTARLDT AIRDVRGSQK VTDQAPESRY SALEKFGMDL TERAKAGKID
PVIGRDEEIR RVVQVLSRRT KNNPVLIGEP GVGKTAIAEG LAQRIINGDV PESLKNRKLI
SLDMGSLIAG AKYRGEFEDR LRAVLKEVIQ SDGQIVLFID ELHTVVGAGA AGQGNMDAGN
LLKPMLARGE LRCIGATTLD EYRKYIEKDA ALERRFQQVM IDQPTVEDTI SILRGLKERY
EVHHGVNITD SALVAAATLS SRYISDRFLP DKAIDLVDEA AAKLRMEITS KPTELEQIER
RLRQLEMEKL SIKSEDKITG LTGLSRNSKD RLERLEQEIS ELQPKKDALD SQWQSEKQIL
ETIKSLKQEE DQLRVQIEQA ERAYDLNTAA QLKYGRLEAL QHDREKQEAQ LIELQAGGST
LLREQVTEAD IAEIVARWTG IPITRLLESE RQKLLNLEGH LHERVIGQHD AVEAVAAAIR
RARSGMKDPS RPIGSFLFMG PTGVGKTELA RALAQFLFDS DDAIVRLDMS EYMEKHSVSR
LVGAPPGYVG YDEGGQLSEA IRRKPYSVVL LDEVEKAHPD VFNILLQVLD DGRITDSQGR
TVDFRNAVIV MTSNIGSEHI LDIAGDEAKY EEMQKRVMTA LRKHFRPEFL NRIDDTILFH
PLSRAELGEI VRLQLIRIQS MLSDQKITLE LSAAAQKYVA DVGYDPTYGA RPLKRAIQRE
LQNPIATKLL ENAFGEGDTI VIDLVEGKLK FSKKELVSSS QTVNTASVAV AERRE
//
