ID A0A0L6CKW4_9MICO Unreviewed; 855 AA.
AC A0A0L6CKW4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=VV01_16400 {ECO:0000313|EMBL:KNX38369.1};
OS Luteipulveratus halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Luteipulveratus.
OX NCBI_TaxID=1631356 {ECO:0000313|EMBL:KNX38369.1, ECO:0000313|Proteomes:UP000037397};
RN [1] {ECO:0000313|Proteomes:UP000037397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C296001 {ECO:0000313|Proteomes:UP000037397};
RA Juboi H., Basik A., Shamsul S.S., Arnold P., Schmitt E.K., Sanglier J.-J.,
RA Yeo T.;
RT "Luteipulveratus halotolerans sp. nov., a novel actinobacterium
RT (Dermacoccaceae) from Sarawak, Malaysia.";
RL Submitted (MAR-2015) 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:KNX38369.1}.
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DR EMBL; LAIR01000002; KNX38369.1; -; Genomic_DNA.
DR RefSeq; WP_050670819.1; NZ_LAIR01000002.1.
DR AlphaFoldDB; A0A0L6CKW4; -.
DR STRING; 1631356.VV01_16400; -.
DR PATRIC; fig|1631356.3.peg.3255; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000037397; 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 Reference proteome {ECO:0000313|Proteomes:UP000037397};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 405..485
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 855 AA; 92324 MW; 7732E8DE01E1EE71 CRC64;
MDLQLTTKAQ EALASAVRHA TTAGQPQVEP AHLLLALTEQ TDTTTAPLLE AAGTTVAAAR
SAAESAIAAM PAASGSSVAQ PSMSRALLNV LEQARELMTS MGDTFVSTDH LLVATARIGD
LGLDAAAIEQ AIPATRGGAK VTSAEPEGTF EALEKYGTDL TAAAREGRLD PVIGRDSEIR
RVVQVLSRRT KNNPVLIGDP GVGKTAVVEG LAQRIVEGDV PESLRDKRLI SLDLGAMVAG
AKYRGEFEER LKAVLEEIKG SDGEVVTFID ELHTVVGAGA SGEGAMDAGN MLKPMLARGE
LRLVGATTLD EYREHIEKDA ALERRFQQVF VGEPSVEDTI AILRGLKERY EAHHKVAIAD
SALVAAASLS DRYITSRQLP DKAIDLIDEA ASRLRMEIDS SPVEIDELRR AVDRLKMEEL
HLQNETDDAS RERLSRLQSD LADKQEQLAA LTARWDAEKA GLNRVGDIKA RIDELRTQAD
RLQREGDYAG ASKLLYGDLP ALEADLTSAQ EAEATSSTAG GDAPMVKEEV EADDIADVIS
SWTGIPAGRL LEGETEKLLK MESVIGERLI GQSDAVAAVS DAVRRSRAGV ADPDRPTGSF
LFLGPTGVGK TELAKSLAEF LFDDERAMVR IDMSEYSERH AVARLIGSPP GYVGYEEGGQ
LTEAVRRRPY SVVLLDEVEK AHPETFDILL QVLDDGRLTD GQGRTVDFRN VILVMTSNLG
SQFLIDPTLS DEAKRESVMG AVRSAFKPEF LNRLDEVVIF DPLSQDELAH IVDLQVAALS
ARLADRRISL QVTDAARHWL AQQGYDPAYG ARPLRRLVQK EIGDRLARAL LAGEVRDGQQ
VRVDKPADAE GLTLA
//
