GenomeNet

Database: UniProt
Entry: A0A1H1LVQ8_9CELL
LinkDB: A0A1H1LVQ8_9CELL
Original site: A0A1H1LVQ8_9CELL 
ID   A0A1H1LVQ8_9CELL        Unreviewed;       867 AA.
AC   A0A1H1LVQ8;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN04489860_0043 {ECO:0000313|EMBL:SDR78517.1};
OS   Paraoerskovia marina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Paraoerskovia.
OX   NCBI_TaxID=545619 {ECO:0000313|EMBL:SDR78517.1, ECO:0000313|Proteomes:UP000185663};
RN   [1] {ECO:0000313|EMBL:SDR78517.1, ECO:0000313|Proteomes:UP000185663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22126 {ECO:0000313|EMBL:SDR78517.1,
RC   ECO:0000313|Proteomes:UP000185663};
RA   de Groot N.N.;
RL   Submitted (OCT-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. {ECO:0000256|RuleBase:RU362034}.
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   ---------------------------------------------------------------------------
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; LT629776; SDR78517.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1LVQ8; -.
DR   STRING; 545619.SAMN04489860_0043; -.
DR   eggNOG; COG0542; Bacteria.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000185663; Chromosome i.
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 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   Hydrolase {ECO:0000313|EMBL:SDR78517.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDR78517.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185663};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..530
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   867 AA;  93770 MW;  860F79329FAFC5C0 CRC64;
     MDAKFTTMSQ QAIGDAIQSA SAAQNPQLEP VHLLGSLLAQ DTGVARGLLD AVGADTQAIG
     QKVRAQLVAL PAASGSAVAQ PTASRGTSAA LDLAQKEAEA LGDEYVSTEH LLIGLAAGSS
     PAAQILADAG ASADSLRSAL PSVRGNGRVT SPNPEGTYKA LEQYGLDLTA RAREGRLDPV
     IGRDAEIRRV VQVLSRRTKN NPVLIGDPGV GKTAVVEGLA QRIVAGDVPT SLQGKRLISL
     DLAAMVAGAK YRGEFEERLK AVLEEITASD GEVVTFIDEL HTVVGAGAGG EGAMDAGNML
     KPMLARGELR LVGATTLDEY REHVEKDPAL ERRFQQVYVG EPTVEDTVAI LRGLKERYEA
     HHKVTIADSA LVAAAALSDR YITSRQLPDK AIDLVDEAAS RLRMEMDSSP IEIDELQRAV
     TRLEMEEVVL KESDDDASVD RLEKLRADLA DRREELAGLT ARWEQEKAGH NRIGELRARI
     DELRTEAERF QRENDLESAA RLLYGEIPQV ERQLAEAEHE EATKDASEAQ DPMVAEKVGA
     DEIAEVVSSW TGIPAGRMLQ GESEKLLHME DVIADRLIGQ RAAVASVSDA VRRSRAGVAD
     PDRPTGSFLF LGPTGVGKTE LAKSLADFLF DDERAMVRID MSEYAEKHSV ARLVGAPPGY
     VGYEEGGQLT EAVRRRPYSV VLLDEVEKAH PEVFDILLQV LDDGRLTDGQ GRTVDFRNVI
     LVLTSNLGSQ FLVDPTLDES VKRESVMTAV RASFKPEFLN RLDDVVIFDP LNITELGRIV
     EIQVSALAAR LADRRITLDV TDDAREWLAL EGFDPAYGAR PLRRLVQREI GDRLARLLLA
     GQVPDGSTVR VDRPSDGDEP GLALSVV
//
DBGET integrated database retrieval system