ID A0A251WB88_9CYAN Unreviewed; 874 AA.
AC A0A251WB88;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=B0A82_20095 {ECO:0000313|EMBL:OUC12860.1};
OS Alkalinema sp. CACIAM 70d.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Alkalinema.
OX NCBI_TaxID=1934309 {ECO:0000313|EMBL:OUC12860.1, ECO:0000313|Proteomes:UP000194922};
RN [1] {ECO:0000313|EMBL:OUC12860.1, ECO:0000313|Proteomes:UP000194922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CACIAM 70d {ECO:0000313|EMBL:OUC12860.1};
RA Lima A.R., Siqueira A.S., Pereira J.S., Goncalves E.C.;
RT "Draft genome of Alkalinema sp. CACIAM 70d.";
RL Submitted (JAN-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}.
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:OUC12860.1}.
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DR EMBL; MUGG01000168; OUC12860.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A251WB88; -.
DR STRING; 1934309.B0A82_20095; -.
DR Proteomes; UP000194922; 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 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:UP000194922};
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"
SQ SEQUENCE 874 AA; 98315 MW; C13770FF978E7F32 CRC64;
MQPSNPNQFT EKAWEAIGRT PDIVKQANQQ QIETEHLMKA LLEQDGLAAS VFNKLGVSVQ
RLRDRTEEYI AKQPKVSGAN QNVYFGRSSD SLLDRAESYR KQYGDDFISV EHMLLGYAQD
SRFGKALFAE FKLDEAKLKA AIEQIRGNQK VTDQNPEGKY EVLEKYGRDL TKYAKEGKLD
PVIGRDDEIR RTIQILSRRT KNNPVLIGEP GVGKTAIAEG LAQRIVSGDV PQSLKDRTLI
ALDMGALIAG AKYRGEFEER LKAVLKEVTD SQGNIILFID EIHTVVGAGA TQGAMDAGNL
LKPMLARGEL RCIGATTLDE YRKYIEKDAA LERRFQQVYV DQPSVEDTIS ILRGLKERYE
LHHGVKISDS SLVAAATLST RYISDRFLPD KAIDLVDEAA AKLKMEITSK PEQLDEVDRK
ILQLEMERLS LQKESDVASK ERLQRLEKEL ADLKEEQSRL NAQWQAEKGG IGELQKIKEE
IDRVNLEVQQ AERDYDLNRA AELKYGTLAQ LQKKLEATEA KLTATQTTGK SLLREEVTES
DIAEIISKWT GIPISKLVQS EMQKLLHLED ELHDRVIGQN EAVTAVADAI QRSRAGLADP
NRPIASFIFL GPTGVGKTEL AKALAAYLFD TEDAMVRIDM SEYMEKHAVS RLIGAPPGYI
GYDEGGQLTE AVRRRPFSVI LFDEIEKAHP DVFNVMLQIL DDGRVTDSQG RTVDFKNTII
IMTSNIGSQY ILDVAGDDSR YEEMRSRVME AMRGSFRPEF LNRVDETIIF HSLQKDEIRN
IIRLQVQRLA KRLDDRKMTL KLSDAALDFL ADIGYDPVYG ARPIKRAIQK EVETAIAKCI
LRGEFSEGDT IFVDVGATER LEFKRLPSEL TVTQ
//