ID A0A2T1CYG6_9CYAN Unreviewed; 892 AA.
AC A0A2T1CYG6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PSB13299.1};
GN ORFNames=C7B76_20325 {ECO:0000313|EMBL:PSB13299.1};
OS filamentous cyanobacterium CCP2.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107700 {ECO:0000313|EMBL:PSB13299.1, ECO:0000313|Proteomes:UP000239512};
RN [1] {ECO:0000313|EMBL:PSB13299.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB13299.1,
RC ECO:0000313|Proteomes:UP000239512};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB13299.1, ECO:0000313|Proteomes:UP000239512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCP2 {ECO:0000313|EMBL:PSB13299.1,
RC ECO:0000313|Proteomes:UP000239512};
RA Keele B.F.;
RL Submitted (MAR-2018) 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:PSB13299.1}.
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DR EMBL; PVWD01000170; PSB13299.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1CYG6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000239512; 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 Reference proteome {ECO:0000313|Proteomes:UP000239512};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 4..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..536
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 892 AA; 100069 MW; 6C8A7E58059992FD CRC64;
MQPTDESKFT EKAWDAIVKS QDVARRFRHQ NLEVEHLVIA LLGQEEGLAS TLLGKAGVDI
ARFKQQIEGY AQRQPRVTYD NTLYLGQGLD SLLDRAEEVR KGMQDDFISI EHILLALAED
ERIGRRFFRD NNANIRQLEA AIKAARGTQK VKDRNPETGY AALEKFGIDL TDRARAGKLD
PVIGRDEEIR RVIQVLSRRT KNNPVLIGEP GVGKTAIAEA LAQRIINGDV PESLKNRRLI
SLDMGSLIAG AKYRGEFENR LRSVLREVTG SEGQIVLFID ELHTVVGAGS AQGSTDAGNL
LKPMLARGEL RCIGASTLDE YRKYIEKDAA LERRFQQVYI GQPSVEDTIS ILRGLKERYE
VHHGVKIADS SLVAAATLSD RYISDRFLPD KAIDLVDEAA AKLKMEITSK PVELETIERR
LIQLEMEKLS LEGEGNSSIA IGVYRTSKDR LEKIEQEIDT LKAEQDKLSS QWQLEKDLLE
AINTLKEEEE NLRRQIEKAE RDYDLNTAAQ LKYGRLASLH DELELKESSL LEIQNRGMTL
LREQVTESDI AEIVAKWTGI PVNRLMESER QKLLQLESFL HQRVIGQQEA VEAVAAAIRR
ARAGMKDPGR PIGSFMFLGP TGVGKTELAR ALAECLFDTD EALVRLDMSE YMEKNSVARL
VGAPPGYVGY EEGGQLSEAI RRHPYSVLLL DEVEKAHPDV FNILLQLLDD GRITDSQGRV
ADCRNTIVVM TSNIGSEHIL DVSGDDAQYD EMQKRVMQAL RSHFRPEFLN RVDDIILFHA
LSITELRQIV GIQLLRVRRM LAEQKIGLEL SVAAQNYVAD VGYDPVYGAR PLKRAIQKEI
ENPIATKILE NTFVEGDTIY VEVVEHKLAF NKKNSALSGQ PSAIPQVLRA ES
//
