ID A0A5M3WPP8_9ACTN Unreviewed; 875 AA.
AC A0A5M3WPP8;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB_1 {ECO:0000313|EMBL:GES08218.1};
GN Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=Amac_018130 {ECO:0000313|EMBL:GES08218.1};
OS Acrocarpospora macrocephala.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Acrocarpospora.
OX NCBI_TaxID=150177 {ECO:0000313|EMBL:GES08218.1, ECO:0000313|Proteomes:UP000331127};
RN [1] {ECO:0000313|EMBL:GES08218.1, ECO:0000313|Proteomes:UP000331127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16266 {ECO:0000313|EMBL:GES08218.1,
RC ECO:0000313|Proteomes:UP000331127};
RA Ichikawa N., Kimura A., Kitahashi Y., Komaki H., Oguchi A.;
RT "Whole genome shotgun sequence of Acrocarpospora macrocephala NBRC 16266.";
RL Submitted (OCT-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|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:GES08218.1}.
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DR EMBL; BLAE01000009; GES08218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5M3WPP8; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000331127; 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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
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 424..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 875 AA; 95503 MW; E06D7966C5DCEDCA CRC64;
MDYKLTQKSQ EALAGAMRRA AAEGNPEISP AHLLTTLLAQ TGGTAVPLLE AVGADWKVLR
TQAEHLLAGL PKAQGATVAA PATSRQLLTV LNTAAQRAKQ LEDDYVSTEH LLVGLATDGG
AVADLLKAQG ATSSALLDAF EKVRGHARVT SETPEDTYQA LEKYGVDLTE RARNGKLDPV
IGRDAEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRMVAGDVPE SLRNKRLVSL
DLGAMVAGAK YRGEFEERLK AVLNEIKESD GQIVTFIDEL HTMVGAGAAE GAMDAGNMLK
PMLARGELRM IGATTLDEYR ERIEKDPALE RRFQQVYVGE PSAEDTIAIL RGLKGRYEAH
HQVQISDGAL VAAATLSDRY ITARFLPDKA IDLVDEAASR LRMEIDSRPV EIDALQRVVD
RMKMEELALA KETDEASLQR LEKLREELAN RQEDLNGLVG RWEQEKAGLN RVGDLKKQLD
DSRSTAERAQ RDGKFEEAAR LMYGEVPRLE KELAEATHAA QREQTMVKEE VGPDDIAEVI
SAWTGIPAGR LLEGETAKLL RMEEELGKRL IGQRAAVQAV SDAVRRARAG VSDPDRPTGS
FLFLGPTGVG KTELAKALAD FLFDDERAMT RIDMSEYSEK HSVARLVGAP PGYVGYEEGG
QLTEAVRRRP YTVVLLDEVE KAHPEVFDIL LQVLDDGRLT DGQGRTVDFR NTILILTSNI
GSQFLVDPQL ENGAKREAVM GAVRTAFKPE FLNRLDDVIL FDALGSEELS QIVDLQVEHL
ARRLAARRLT LTVTAAARDW LSLTGYDPMY GARPLRRLVQ SAIGDQLAKE LLAGQVRDGE
EVIVDLDEGA DSLVVRPARS AAPVPEDAGA PGDRP
//
