ID A0A502CLU2_9SPHN Unreviewed; 859 AA.
AC A0A502CLU2;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-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:TPG13594.1};
GN ORFNames=EAH84_05250 {ECO:0000313|EMBL:TPG13594.1};
OS Sphingomonas oligophenolica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=301154 {ECO:0000313|EMBL:TPG13594.1, ECO:0000313|Proteomes:UP000318413};
RN [1] {ECO:0000313|EMBL:TPG13594.1, ECO:0000313|Proteomes:UP000318413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5.1 {ECO:0000313|EMBL:TPG13594.1,
RC ECO:0000313|Proteomes:UP000318413};
RX PubMed=31206918;
RA Altshuler I., Hamel J., Turney S., Magnuson E., Levesque R., Greer C.,
RA Whyte L.G.;
RT "Species interactions and distinct microbial communities in high Arctic
RT permafrost affected cryosols are associated with the CH4 and CO2 gas
RT fluxes.";
RL Environ. Microbiol. 0:0-0(2019).
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:TPG13594.1}.
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DR EMBL; RCZK01000003; TPG13594.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A502CLU2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000318413; 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:UP000318413};
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; 93677 MW; A1348663407C0EFC CRC64;
MNLEKFTDRA KGFLQSAQTV AIRMNHQRIA PEHLLKALLE DDQGMAAGLV TAAGGDARKA
TSETDLALSK IPAVSGSGAQ QTPGLDNDAV RVLDSAEQIA AKAGDSYVTV ERLLVALALG
LNAAAGKALK AAGATPEKLN AAINDLRGGR TADTASAEDR YDALKKFARD LTQAARDGKL
DPVIGRDEEI RRTIQILARR TKNNPALIGE PGVGKTAIAE GLALRIANGD VPDTLKGRTL
MSLDMGALIA GAKYRGEFEE RLKGVLDEVK AADGDIVLFI DEMHQLIGAG KSEGAMDAGN
LLKPALARGE LHCVGATTLD EYRKYVEKDP ALQRRFQPVF VGEPTVEDTI SILRGLKDRY
ELHHGVRITD ASLVAAATLS NRYITDRFLP DKAIDLMDEA ASRIRMEVES KPEEIETLDR
RIIQLKIERE ALRRETDAAS VDRLATLEGD LANLEQQSSE LTTRWQAEKD KIGAEAKLKE
QLDAARIELD QAQREGNLAR AGELSYGTIP QLSKQLDDAQ GQTKGAMLRE EVTADDIAGV
VSRWTGIPVD RMLQGERDKL LRMEEVIGKR VIGQAEAVRA VSTAVRRARA GLQDANRPLG
SFLFLGPTGV GKTELTKALA EFLFDDGNAM VRIDMSEFME KHAVARLIGA PPGYVGYEEG
GVLTEAVRRR PYQVVLFDEV EKAHGDVFNI LLQVLDDGRL TDGQGRTVDF SNTLIILTSN
LGSQYLANLD EGQDVESVEP QVMEIVRGHF RPEFLNRLDD IILFHRLGQA HMAPIVDIQV
ARVDKLLADR KITLALTDAA RAWLGRVGYD PVYGARPLRR AVQRYLQDPL ADLILRGDVK
DGSTVDVDES DGKLTLTVV
//