ID A0A2A8CTQ9_9BACT Unreviewed; 893 AA.
AC A0A2A8CTQ9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:PEN11079.1};
GN ORFNames=CRI94_16795 {ECO:0000313|EMBL:PEN11079.1};
OS Longibacter salinarum.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC Longibacter.
OX NCBI_TaxID=1850348 {ECO:0000313|EMBL:PEN11079.1, ECO:0000313|Proteomes:UP000220102};
RN [1] {ECO:0000313|EMBL:PEN11079.1, ECO:0000313|Proteomes:UP000220102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 52045 {ECO:0000313|EMBL:PEN11079.1,
RC ECO:0000313|Proteomes:UP000220102};
RA Goh K.M., Shamsir M.S., Lim S.W.;
RT "Draft genome of Longibacter Salinarum.";
RL Submitted (OCT-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|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:PEN11079.1}.
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DR EMBL; PDEQ01000012; PEN11079.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A8CTQ9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000220102; 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:UP000220102};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 405..530
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 893 AA; 99505 MW; BC1FB86E81CEE1E4 CRC64;
MNLQKFTVKA QEAVQSAMEI AASNNHQGVE PAHVLKAFLS DTEGITTSIL RRLGASVDTL
RQRTDSALDK LPKVTGASVS GQYLGDELKK VFDRARAEAD LMNDEYVSTE HLLIGLVESK
GEVGQALRDQ GASKDKVRDV LEDVRGGQSA DDPHAESRYE ALDRFARDLN DLARRGKIDP
VIGRDQEIRR VLQILSRRTK NNPVLVGEAG VGKTAIAEGI ATRIVQGDVP ESMKSKRIVA
LDMGALVAGA KYRGEFEDRL KAVVKEVSES DGELILFIDE LHTLIGAGAA EGAMDAANIL
KPALARGELR AIGATTLDEY KYIEDDRALE RRFQKVVVDE PSVDDTISIL RGLKERYEVH
HGVRIQDSAI ISAADLSNRY ITDRQLPDKA IDLIDEAAAR LRIEIDSMPA DLDQLDREIR
QLEIEREAIK RDEDEEKLEN INHQIASLED ERDALKTRWK EEKDLIQTAR QAKEKIDELR
VEAENLEREG KYDRVAEIRY GEIPDLEKQA EEANEKLQEV QQDGALLKEE VDGEDIAEIV
SNWTGIPVSK MLESERQKLV RMEEELSKRV IGQPEAIEVV SDAVRRGRTG LQEENRPIGS
FLFLGTTGVG KTELAKTLAA FLFNDEDAMV RIDMSEYQEK HTASRLIGAA PGYVGYEEGG
QLTEAVRRKP YSVVLLDEIE KAHPEIFNVL LQVLDDGRLT DNQGRTVDFT NTIIIMTSNM
GSEVITEKMD SVDGGYLSDL ERQELEEKLL KMLRQRLRPE FLNRIDEVVT FRSLGRSHIR
EIVELQFNRI AGIAKKSHNL QLQLSDAAKD WLADRGFDPA FGARPLKRVM QRQVSNQLSK
ELLGGSVEDG DTVRIDLAPE QNHLTFEAVR TGADGTGEAA ETAEPAGDGA VSM
//