ID A0A432VFB7_9SPHN Unreviewed; 859 AA.
AC A0A432VFB7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RUN75375.1};
GN ORFNames=EJC47_16605 {ECO:0000313|EMBL:RUN75375.1};
OS Sphingomonas sp. TF3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=2495580 {ECO:0000313|EMBL:RUN75375.1, ECO:0000313|Proteomes:UP000275325};
RN [1] {ECO:0000313|EMBL:RUN75375.1, ECO:0000313|Proteomes:UP000275325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF3 {ECO:0000313|EMBL:RUN75375.1,
RC ECO:0000313|Proteomes:UP000275325};
RA Afonin A., Vasilieva E., Akhtemova G., Zhukov V.;
RT "The Draft Genome Sequence of a Sphingomonas sp strain TF3.";
RL Submitted (DEC-2018) 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:RUN75375.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RWKS01000021; RUN75375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A432VFB7; -.
DR Proteomes; UP000275325; 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:UP000275325};
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; 93907 MW; 77EE4BC03E494635 CRC64;
MNIEKFTDRA KGFLQSAQTV AIRMSHQRIA PEHILKALLE DEQGMASGLI AAAGGDAKRA
ATETDLALSK IPAVSGSGAQ QTPGLDNDAV RVLDQAEQIA TKSGDSFVTV ERLLVALALS
LNTAAGKALK TAGVTPEALN TAIEQVRNGR VADSASAEDK FDALKKFARD LTQAARDGKL
DPVIGRDEEI RRTIQILARR TKNNPVLIGE PGVGKTAIAE GLALRIANGD VPDTLKDRRL
MSLDMGSLIA GAKYRGEFEE RLKGVLDEVK AAEGDIVLFI DEMHQLIGAG KSEGAMDAGN
LLKPALARGE LHCVGATTLD EYRKYVEKDA ALQRRFQPVF VGEPTVPDTI SILRGLKEKY
ELHHGVRITD AAIVAAATLS NRYITDRFLP DKAIDLMDEA ASRIRMEVES KPEEIEILDR
RIIQLKIERE ALKRESDEAS RDRLVKLDAE LANLEQQSSE LTTRWQGEKD KISAEAKLKE
QIDAARLELE QAQRAGDLAK AGELSYGRIP ELQRQLDAAA GATKGAMLRE EVTSEDIAGV
VARWTGIPVE RMLEGERDKL LQMEATIGKR VIGQQNAIRA VSTAVRRARA GLQDPNRPLG
SFLFLGPTGV GKTELTKALA EFLFDDPTAM VRIDMSEFME KHAVARLIGA PPGYVGYEEG
GVLTEAVRRR PYQVVLFDEV EKAHGDVFNI LLQVLDDGRL TDGQGRTVDF TNTIIVLTSN
LGSQILTTLG EGEDVASVEP QVMEIVRGHF RPEFLNRLDE IVLFHRLGQA EMAPIVDIQV
QRIATLLAER KVSLELTDAA RAWLGRVGYD PVYGARPLKR AVQRYLQDPL ADLILRGSVK
DGATVRVDEG DGRLELAVE
//