ID A0A2A9EE39_9MICO Unreviewed; 874 AA.
AC A0A2A9EE39;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ATL41_1821 {ECO:0000313|EMBL:PFG37073.1};
OS Flavimobilis soli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae;
OC Flavimobilis.
OX NCBI_TaxID=442709 {ECO:0000313|EMBL:PFG37073.1, ECO:0000313|Proteomes:UP000221394};
RN [1] {ECO:0000313|EMBL:PFG37073.1, ECO:0000313|Proteomes:UP000221394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21574 {ECO:0000313|EMBL:PFG37073.1,
RC ECO:0000313|Proteomes:UP000221394};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) 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 -!- 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:PFG37073.1}.
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DR EMBL; PDJH01000001; PFG37073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A9EE39; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000221394; 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 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:PFG37073.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PFG37073.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000221394};
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 423..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 874 AA; 94122 MW; 8CDA97119C2E8F8B CRC64;
MDPKFTTKSR EALEDAIQTA TAAGNPEVEP IHVLAGLLGQ TDGLAPQLLA AAGVDASTVG
RDVRKALTDL PSATGGGVTQ PGLADATKRL ITAASTEMQA LGDEYVSAEH LLIAAADVAS
SAATILRRAG ASPDALRAAL PSVRGNTKVT SPNPEGTYKS LEKYGVDLTA AAREGKLDPV
IGRDSEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPE SLRGKRIVSL
DLPAMVAGAK YRGDFEERLK AVLSEIKESD GEIVTFIDEL HTVVGAGAGG EGAMDAGNML
KPMLARGELR LVGATTLDEF REHIEKDPAL ERRFQQVYVG EPSVEDTVAI LRGLKSRYEA
HHRVTISDGA LVAAATLSDR FISGRQLPDK AIDLVDEAAS RLRMEMDSSP VEIDTLRRVV
TRLEMELMQI SKSEDEADKA RADELRAQLA DRREELAALN ARWETEKGGL NRVGDLHKKL
DELRSAADRA ELEGDLETTS RIRYGEIPEL EREIAAAEEA QRAAVPDPEA GQEVELAQAR
PPKLVGDKVD AAEIAEVVSA WTGIPAGRLL QGESQKLLSM EQTIGARLIG QTAAVASVSD
AVRRSRAGIN DPDRPIGSFL FLGPTGVGKT ELAKSLADFL FDDERAMVRI DMSEYGEKHS
VARLVGAPPG YVGYEEGGQL TEAVRRRPYS VVLLDEVEKA HPEVFDLLLQ VLDDGRLTDG
QGRTVDFRNT ILVMTSNLGS HALVDPLVAE GDKREAVMAA VRAHFKPELL NRLDDVIVFD
PLTITELSQI VDIQVRALAA RLAERRLTLD VTDAAREWLA LEGFDPAYGA RPLRRLVQRE
IGDRLARALL SGAIGDGDTV RVDRGPDGLT VERA
//