ID A0A1N6H5S1_9SPHN Unreviewed; 859 AA.
AC A0A1N6H5S1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN02745824_3146 {ECO:0000313|EMBL:SIO15106.1};
OS Parasphingorhabdus marina DSM 22363.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Parasphingorhabdus.
OX NCBI_TaxID=1123272 {ECO:0000313|EMBL:SIO15106.1, ECO:0000313|Proteomes:UP000185192};
RN [1] {ECO:0000313|Proteomes:UP000185192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22363 {ECO:0000313|Proteomes:UP000185192};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FSQW01000002; SIO15106.1; -; Genomic_DNA.
DR RefSeq; WP_074206064.1; NZ_FSQW01000002.1.
DR AlphaFoldDB; A0A1N6H5S1; -.
DR STRING; 1123272.SAMN02745824_3146; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000185192; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:SIO15106.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SIO15106.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185192};
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; 94291 MW; CA99FA40C54B797F CRC64;
MNLEKFTDRA KGFLQSAQTV AIRMNHQQIA AVHLLKALLE DDQGMASGLI AKAGGNAKQA
HVAVDGALAK IPAVSGGGAQ QTPGLNNDAV RVLDQAEQIS EKAGDSFVTV ERLLLALVLS
KDTEAGKALA EAGVTAEALN SAINDLRGGR TADTASAEDR YEAMKKFARD LTEAARDGKL
DPVIGRDEEI RRTIQILARR TKNNPVLIGE PGVGKTAIAE GMALRIANGD VPDSLKDRRL
MALDMGSLIA GAKYRGEFEE RLKGVLDEVR GADGEIILFI DEMHTLIGAG ASEGAMDASN
LLKPALARGE LHCIGATTLD EYQKHVEKDP ALQRRFQPVV IGEPTVEDTI SILRGLKEKY
ELHHGVRITD GALVSAATLS HRYISDRFLP DKAIDLMDEA ASRIRMEVES KPEEIETLDR
RIIQLKIERE ALSKENDDAS KSRLEALEKE LADLEQESTE LTTRWQGEKD KIHAEAHLKE
ELDAARLELE QAERAGDLAK AGELSYGKIP DLEKKLETAA DATEGAMLRE EVVSEDIASV
VSRWTGIPVD KMLEGEREKL LAMEELISKR VIGQKDAIEA VSAAVRRSRA GLQDPNRPLG
SFLFLGPTGV GKTELTKALA GFLFDDDQAM VRIDMSEFME KHSVARLIGA PPGYVGYDEG
GVLTEAVRRR PYQVILFDEV EKAHGDVFNV LLQVLDDGHL TDGQGRRVDF SNTLIILTSN
LGSQFMANLE EGQKVKDVEP QVMDVVRAHF RPEFLNRLDE IILFHRLAEE HMAPIVEIQV
GRVQKLLKDR KIVLELTDAA KRWLGRVGYD PVYGARPLKR AIQKYLQDPL ADSILRGDIP
DDTIVRIDEG DGALDIKTA
//
