ID A0A4P6PVI1_9ACTN Unreviewed; 871 AA.
AC A0A4P6PVI1;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:QBI52083.1};
GN ORFNames=EKD16_01330 {ECO:0000313|EMBL:QBI52083.1};
OS Streptomonospora litoralis.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=2498135 {ECO:0000313|EMBL:QBI52083.1, ECO:0000313|Proteomes:UP000292235};
RN [1] {ECO:0000313|EMBL:QBI52083.1, ECO:0000313|Proteomes:UP000292235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M2 {ECO:0000313|EMBL:QBI52083.1,
RC ECO:0000313|Proteomes:UP000292235};
RA Khodamoradi S., Hahnke R.L., Kaempfer P., Schumann P., Rohde M.,
RA Steinert M., Luzhetskyy A., Wink J., Ruckert C.;
RL Submitted (FEB-2019) 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}.
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DR EMBL; CP036455; QBI52083.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4P6PVI1; -.
DR KEGG; strr:EKD16_01330; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000292235; Chromosome.
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:UP000292235};
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 412..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 95377 MW; 360F79891CE775D7 CRC64;
MNYKLTTKSQ EAVSTAMRRA TTDGNPQVEP VHLLAALLNQ GEGIIRPLLK EVGASPDDLA
AKTEQAVAGL PAAAGSTVGA PQSARRLIVS LNTAAQRAQQ MEDEFVSTEH LLVGLAADGG
EAARLLNDAG AAPEALLEAF ERVRGPGKVT TQNPEETYQA LEKYGVDLTD RARSGALDPV
IGRDSEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRVVAGDVPE SLRDKRLIAL
DLSAMVAGAK YRGEFEERLK AVLNEIKDSD GRIITFIDEL HTVVGAGAAE GAMDAGNMLK
PMLARGELRM VGATTLDEYR ERIEKDPALE RRFQQVVVGE PSAADTIAIL RGLKGRYEAH
HKVQIADSAL VAAATLSDRY ITARFLPDKA IDLIDESASR LRMEIDSRPV ELDELQRTVD
RLKMEEMALA KESDAASLQR LERLRADLAD RQEELDGLVA RWEQEKAGLN RVGELKERLD
ELRTQADRAQ RDGDFTEASR LMYGEIPQLE KQLEEASSAE EEADETDEPT MVKDEVGADD
VADVVSSWTG IPVGRLMEGE TAKLLRMEEE LGRRLIGQDQ AVAAVSDAVR RARTGISDPD
RPTGSFLFLG PTGVGKTELA KALAEFLFDD ERAIVRVDMS EYSEKHSVSR LVGAPPGYVG
YEEGGQLTEA VRRRPYTVVL LDEVEKAHIE VFDTLLQVLD DGRLTDGQGR SVDFRNTLLI
MTSNLGSQFL VDTALDDRQR REKVMSVVRS TFKPEFLNRL DDLIVFDTLS TEELTRIVDL
QVDRLAARLG ERRLSLDVTS AAREWLALTG YDPVYGARPL RRLVQAAIGD PLAKAMLSAE
LVEGDTVVVD RDEGEDRLSV RSAAVRQPAS A
//