ID A0A4R6JRT7_9ACTN Unreviewed; 862 AA.
AC A0A4R6JRT7;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=C8E87_3058 {ECO:0000313|EMBL:TDO39373.1};
OS Actinoplanes brasiliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=52695 {ECO:0000313|EMBL:TDO39373.1, ECO:0000313|Proteomes:UP000294901};
RN [1] {ECO:0000313|EMBL:TDO39373.1, ECO:0000313|Proteomes:UP000294901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43805 {ECO:0000313|EMBL:TDO39373.1,
RC ECO:0000313|Proteomes:UP000294901};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (MAR-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:TDO39373.1}.
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DR EMBL; SNWR01000001; TDO39373.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R6JRT7; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000294901; 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 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 Hydrolase {ECO:0000313|EMBL:TDO39373.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TDO39373.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 414..501
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 94223 MW; 0166A99B85E2BDBB CRC64;
MNAERLTTKS RDVITGAVAD AGRRGHATVE PWHMLLSLLD TGGSTAPALL RAVGANPADV
RRAALRSVEQ LPSARGASTA EPSLSREFVN AIGEAELIAQ PLRDEYISTE HLLAGLARVG
GAVGRALKDV GATEEALVAA FPQVRGGERR VTNADPEQTY KALEKYSVDL TALAREGKID
PVIGRDAEIR RVVQVLSRRT KNNPVLIGEP GVGKTAIVEG LAQRIVAGDV PETLRDKKLV
SLDLGAMVAG AQYRGQFEER LKSVLEEIRN SNGQVVTFLD ELHTVVGAGK GEGSMDAGNM
LKPMLARGEL RMVGATTLDE YREHIEKDPA LERRFQPVVV GEPTVEDTIG ILRGLKGRYE
AHHRVQITDA ALVAAASLSD RYISDRFLPD KAIDLIDEAA SRLRMEIDSR PVELDQLQRQ
VDRMRVEKLA LEKETDPASR DRLTRLEFDL ANREEELTAL NARWERERGG LNRVGELKKQ
LDETRAELER AQRDADWEKA SRLQYQEIPA LEQELGTASA ADEEAAAEPP MVKEEVGADD
IAEVISSWTG IPAGRMMEGE TAKLLRMEES LREKVVGQAE AVAAVAGAVR RARAGIADPD
RPTGSFLFLG PTGVGKTELA KALAGFLFDD ERAMVRIDMS EYGEKHSVAR LVGAPPGYVG
YEEGGQLTEA VRRRPYSVVL LDEVEKAHPD VFDVLLQVLD DGRLTDGQGR TVDFRNAILV
LTSNLGSQTA DITMGDEERR DEVLAVVRGH FKPEFLNRLD DIVVFHALTR DDLAAIVDIQ
LGRLRTRLAE RRLTLDVSGT AIDWLGEHGY DPIYGARPLR RLVQSTIGDA LAKALLAGEI
RDGDRVVVDL AGSKEGLRVS RG
//
