ID A0A0Q4PW34_9SPHN Unreviewed; 858 AA.
AC A0A0Q4PW34;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ASE90_15930 {ECO:0000313|EMBL:KQN79823.1};
OS Sphingomonas sp. Leaf67.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736230 {ECO:0000313|EMBL:KQN79823.1};
RN [1] {ECO:0000313|EMBL:KQN79823.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf67 {ECO:0000313|EMBL:KQN79823.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN79823.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf67 {ECO:0000313|EMBL:KQN79823.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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:KQN79823.1}.
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DR EMBL; LMLP01000025; KQN79823.1; -; Genomic_DNA.
DR RefSeq; WP_056004362.1; NZ_LMLP01000025.1.
DR AlphaFoldDB; A0A0Q4PW34; -.
DR STRING; 1736230.ASE90_15930; -.
DR Proteomes; UP000051342; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 93695 MW; 9C60F74C72CE0072 CRC64;
MNLEKFTDRA KGFLQAAQTV AIRNSHQRMT PEHILKALLD DEQGMAAGLI TAAGGDARRA
IAEIDAALAK LPAVSGSGAQ QNPGLDNDSV RLLDQAEQIA TKAGDSFVTV ERMLLALTLS
QGPAGKALTT AGLTAQNLNA AIDKLRGGRT ADTAGAEDRY DALRKFARDL TAAARDGKLD
PVIGRDEEIR RTIQILARRT KNNPVLIGEP GVGKTAIAEG LALRIANGDV PEGLKDRALM
SLDMGSLIAG AKYRGEFEER LKGVLDEVKA GDGQIILFID EMHQLIGAGK SEGAMDAGNL
LKPALARGEL HCIGATTLDE YRKHVEKDPA LQRRFQPVFV GEPTVEDTIS ILRGLKEKYE
LHHGVRITDG ALVSAATLSN RYITDRFLPD KAIDLMDEAA SRIRMEVESK PEAIESLDRR
ILRMKIEREA LRRESDAASI DRLDTLEAEL ANLEQQLSEL TTRWQGERDK IASEAKLKEQ
LDAARVALEQ AQRSGDLAKM SELTYGTIPT LEKQLVAAQQ NAGGAMLREE VTADDIAGVV
SRWTGVPVDR MLEGEREKLL AMEDALGKRV IGQREAVRAV ATAVRRSRAG LQDPNRPLGS
FLFLGPTGVG KTELTKSLAE FLFDDPNAMV RIDMSEFMEK HAVSRLIGAP PGYVGYEEGG
KLTEAVRRRP YQVVLFDEVE KAHGDVFNIL LQVLDDGRLT DGQGRTVDFS NTIIILTSNL
GSQYLTNLPD GVDVETVEPQ VMDVVRAHFR PEFLNRLDEI ILFHRLAADH MAPIVDIQVG
RVGRLLAERK VKVEMTDAAR AWLGRVGYDP VYGARPLKRA VQRYLQDPLA DLILRGSVKD
GSTVRVDEGD GALTLSVG
//
