ID A0A0Q6VX44_9ACTN Unreviewed; 862 AA.
AC A0A0Q6VX44;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ASC64_01690 {ECO:0000313|EMBL:KQV77581.1};
OS Nocardioides sp. Root122.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736431 {ECO:0000313|EMBL:KQV77581.1, ECO:0000313|Proteomes:UP000051395};
RN [1] {ECO:0000313|EMBL:KQV77581.1, ECO:0000313|Proteomes:UP000051395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root122 {ECO:0000313|EMBL:KQV77581.1,
RC ECO:0000313|Proteomes:UP000051395};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV77581.1, ECO:0000313|Proteomes:UP000051395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root122 {ECO:0000313|EMBL:KQV77581.1,
RC ECO:0000313|Proteomes:UP000051395};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQV77581.1}.
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DR EMBL; LMDE01000001; KQV77581.1; -; Genomic_DNA.
DR RefSeq; WP_056905781.1; NZ_LMDE01000001.1.
DR AlphaFoldDB; A0A0Q6VX44; -.
DR STRING; 1736431.ASC64_01690; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051395; 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:UP000051395};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 6..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..497
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 93822 MW; 2F5D720850114215 CRC64;
MSQFGAEKFT TRSREVIEAA QLAATTGGNT HTEPIHLLVA LLKQEDGTSR SLVQKAGVDP
AILLAKAEGA QQQLPRASGS TVQQPSASAA LTRVLAQSLD LAGSMKDDYV ATDHLLVAIA
TVESPAQKVL TDAGLSADGL REAITAVRGN RRVTSEAAEA SYESLEKYSV DLTQAAEDGR
LDPVIGRDAE IRRVVQVLSR RTKNNPVLIG EPGVGKTAVV EGLAQRVVAG DVPDSLKGRR
VLSLDLAAMV AGAKYRGEFE ERLKAVLEEI KDAGGQVITF IDELHTVVGA GAGGDSAMDA
GNMLKPMLAR GELHMIGATT LDEYRERIEK DPALERRFQQ VFVGEPSVED TIQILRGIQE
KYEAHHGVRI TDAALVAAAT LSDRYITGRQ LPDKAIDLID EASSRLRMEH ESSPEEIDQL
RRQVERLKME EFALAKETDD ASRERLEVLR KDLADKEEEL RGLETRWERE KDQLQGEGEL
RRQLDTLKIE AEKKLREGDL AGASEIQYGR IPDLEKQIAE VEKAEAVDLE PLVGEEVGAE
QIADVVEAWT GIPTGKMLQG ETAKLLEMES VIGERLIGQR AAVTAVSDAV RRSRAGIADP
NRPTGSFLFL GPTGTGKTEL AKALADFLFD DERAIVRIDM SEYSEKHSVS RLVGAPPGYV
GYDEGGQLTE AVRRRPYSVV LLDEVEKAHP EVFDILLQVL DDGRLTDGQG RTVDFRNTLL
ILTSNLGSNF LVDPILEPVA KKESVMGVVR SHFKPEFLNR LDEVVMFDAL SKDDLAHIVD
LQLALLEKRL AVRRITISVT DAARAWLAET GFDPAYGARP LRRLIQSAIG DPLARRLIAG
EVTDGGSVTV DAGEDGLSLL AG
//