ID I3UXE4_PSEPU Unreviewed; 831 AA.
AC I3UXE4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=YSA_06299 {ECO:0000313|EMBL:AFK70165.1};
OS Pseudomonas putida ND6.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=231023 {ECO:0000313|EMBL:AFK70165.1, ECO:0000313|Proteomes:UP000005268};
RN [1] {ECO:0000313|EMBL:AFK70165.1, ECO:0000313|Proteomes:UP000005268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND6 {ECO:0000313|EMBL:AFK70165.1,
RC ECO:0000313|Proteomes:UP000005268};
RX PubMed=22933774; DOI=10.1128/JB.01190-12;
RA Li S., Zhao H., Li Y., Niu S., Cai B.;
RT "Complete Genome Sequence of the Naphthalene-Degrading Pseudomonas putida
RT Strain ND6.";
RL J. Bacteriol. 194:5154-5155(2012).
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}.
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DR EMBL; CP003588; AFK70165.1; -; Genomic_DNA.
DR AlphaFoldDB; I3UXE4; -.
DR KEGG; ppi:YSA_06299; -.
DR PATRIC; fig|231023.4.peg.3027; -.
DR HOGENOM; CLU_005070_4_0_6; -.
DR Proteomes; UP000005268; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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 InterPro; IPR002078; Sigma_54_int.
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.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 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}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..123
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 547..783
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT COILED 389..469
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 831 AA; 92394 MW; 776998DDEEAB3838 CRC64;
MDHPAIEPVH LLQALLEQQG GSIKPLLMQV GFDINGLRQG LVKELDQLPK IQNPTGDVNM
SQDLARLLNQ ADRLAQQKGD QFISSELVLL AAMDENSKLG KLLLSQGVSK KALENAINNL
RGGAAVNDAN AEESRQALDK YTVDLTKRAE EGKLDPVIGR DDEIRRTVQV LQRRTKNNPV
LIGEPGVGKT AIAEGLAQRI INGEVPDGLK GKRLLALDMG ALIAGAKYRG EFEERLKSLL
NELSKQEGQI ILFIDELHTM VGAGKGEGAM DAGNMLKPAL ARGELHCVGA TTLNEYRQFI
EKDAALERRF QKVLVEEPSE EDTIAILRGL KERYEVHHKV AITDGAIIAA AKLSHRYITD
RQLPDKAIDL IDEAASRIRM EIDSKPEVLD RLDRRLIQLK VESQALKKEE DEAAKKRLEK
LTEEIERLER EYSDLEEIWA SEKAEVQGSA QIQQKIEQAR QELETARRKG DLSRMAELQY
GVIPDLERSL QMVDQHGKTE NQLLRNKVTE EEIAEVVSKW TGIPVAKMLE GEREKLLKME
ELLHQRVIGQ SEAVTAVANA VRRSRAGLSD PNRPSGSFLF LGPTGVGKTE LCKALAEFLF
DTEEAMVRID MSEFMEKHSV ARLIGAPPGY VGYEEGGYLT EAVRRKPYSV VLLDEVEKAH
PDVFNVLLQV LEDGRLTDSH GRTVDFRNTV IVMTSNLGSA QIQELVGDRE AQRAAVMDAV
GAHFRPEFIN RIDEVVVFEP LGREQIAGIT EIQLGRLRSR LLERELSLSL SPEALDKLIA
VGYDPVYGAR PLKRAIQRWI ENPLAQLILA GKFLPGTAIT AKVEGDEIVF G
//
