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Database: UniProt
Entry: A0A0Q4KGP5_9SPHN
LinkDB: A0A0Q4KGP5_9SPHN
Original site: A0A0Q4KGP5_9SPHN 
ID   A0A0Q4KGP5_9SPHN        Unreviewed;       859 AA.
AC   A0A0Q4KGP5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=ASE86_02750 {ECO:0000313|EMBL:KQN25194.1};
OS   Sphingomonas sp. Leaf33.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736215 {ECO:0000313|EMBL:KQN25194.1, ECO:0000313|Proteomes:UP000051455};
RN   [1] {ECO:0000313|EMBL:KQN25194.1, ECO:0000313|Proteomes:UP000051455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf33 {ECO:0000313|EMBL:KQN25194.1,
RC   ECO:0000313|Proteomes:UP000051455};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN25194.1, ECO:0000313|Proteomes:UP000051455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf33 {ECO:0000313|EMBL:KQN25194.1,
RC   ECO:0000313|Proteomes:UP000051455};
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|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:KQN25194.1}.
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DR   EMBL; LMLB01000001; KQN25194.1; -; Genomic_DNA.
DR   RefSeq; WP_056422039.1; NZ_LMLB01000001.1.
DR   AlphaFoldDB; A0A0Q4KGP5; -.
DR   STRING; 1736215.ASE86_02750; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000051455; 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:UP000051455};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          415..495
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   859 AA;  93725 MW;  F19370A747D6F5B7 CRC64;
     MNLEKFTDRA KGFLQSAQTV AIRMSHQQIA PEHLLKALLE DEQGMAAGLI QAAGGDAKKA
     VAETDLALSK VPVVSGGGAQ QTPGLNNDAV RVLDQAEQIA QKVGDSYVTV ERLLVALALS
     LTTPAGKALQ AAGASADKLN ASIVQMRGGR TADTAGAEDR YDALKKFARD LTQAARDGKL
     DPVIGRDEEI RRTIQILARR TKNNPVLIGE PGVGKTAIAE GLALRIANGD VPDTLKDRKL
     MALDMGSLIA GAKYRGEFEE RLKGVLDEVK AGEGDIILFI DEMHTLVGAG KTDGAMDASN
     LLKPALARGE LHCIGATTLD EYRKYVEKDP ALQRRFQPVY ADEPTVEDTI SILRGLKEKY
     ELHHGVRITD GAIVAAATLS NRYITDRFLP DKAIDLMDEA ASRIRMEVES KPEEIENLDR
     RIIQLKIERE ALKRESDQAS RDRLATLEGD LANLEQQSAE LTTRWQGEKD KIASEAKLKE
     TIEAAKLELE QAQRSGDLAK MSELSYGTLP ALQKQLDDAQ AQTGAAMLRE EVTADDIAGV
     VGRWTGIPVE RMLTGEREKL LRMEEVIGKR VIGQADAVRA VSTAVRRSRA GLQDPNRPLG
     SFLFLGPTGV GKTELTKALA EFLFDDASAM VRIDMSEFME KHAVARLIGA PPGYVGYEEG
     GVLTEAVRRR PYQVVLFDEV EKAHGDVFNV LLQVLDDGRL TDGQGRTVDF SNTLVILTSN
     LGSQYLANLE DGQDVASVEP QVMDIVRSHF RPEFLNRLDE IILFHRLAAD HMAPIVDIQI
     ARLGKLLADR KVTVELSEAA KAWLGRVGYD PVYGARPLKR AVQRYLQDPL ADLILRGDVR
     DGATVRADEG DGKLVLSVG
//
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