ID A0A1I2KKE7_9ACTN Unreviewed; 860 AA.
AC A0A1I2KKE7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05421541_11767 {ECO:0000313|EMBL:SFF66993.1};
OS Actinoplanes philippinensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=35752 {ECO:0000313|EMBL:SFF66993.1, ECO:0000313|Proteomes:UP000199645};
RN [1] {ECO:0000313|EMBL:SFF66993.1, ECO:0000313|Proteomes:UP000199645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43019 {ECO:0000313|EMBL:SFF66993.1,
RC ECO:0000313|Proteomes:UP000199645};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FONV01000017; SFF66993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2KKE7; -.
DR STRING; 35752.SAMN05421541_11767; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199645; 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 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 Hydrolase {ECO:0000313|EMBL:SFF66993.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFF66993.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199645};
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..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 94096 MW; C417313C7DBC1DAB CRC64;
MNTERLTTKS REVITGAVAD AGRRGHATVE PWHMLQSLLD TGGSTATALL RAVGANPAEI
RRAAVRAIEQ LPSARGASTV EPSLSREFVN AIGSADLIAK PLGDEYVSTE HLLAGLARVG
GAVSQVLKDA GATEEALVGA FPQVRGGERR VTTADPEQTY KSLEKYGVDL TALAREGKID
PVIGRDAEIR RVVQVLSRRT KNNPVLIGEP GVGKTAIVEG LAQRIVAGDV PESLRDKKLV
SLDLGAMVAG AQYRGQFEER LKSVLEEIRG SNGQVVTFLD ELHTVVGAGK GEGSMDAGNM
LKPMLARGEL RMVGATTLDE YREHIEKDPA LERRFQPVVV GEPTVEDTIG ILRGLKGRYE
AHHRVQITDA ALVAAASLSD RYISDRFLPD KAIDLIDEAA SRLRMEIDSR PVALDQLHRQ
VDRMRVERLA LEKETDPASM ARLERLIADL ADREEELTAL TARWERERGG LNRVGELKKE
LDEARAAQER AQRDGELLEA SRLLYEVIPT LEREIQRAAE SEEEENTEPP MVKEEVGADD
IAEVVSSWTG IPAGRMMEGE TAKLLRMEDS LAGKVIGQRE AIEAVAGAVR RARAGIADPD
RPTGSFLFLG PTGVGKTELV KALAGFLFDD ERAMVRIDMS EYAEKHSVAR LVGAPPGYVG
YEEGGQLTEA VRRRPYSVVL LDEVEKAHPD VFDLLLQVLD DGRLTDGQGR TVDFRNAILV
LTSNLGSANS DFTMSDEERH DEVLAAVRAH FKPEFLNRLD DIVVFHALTK SDLTRIVDIQ
LARLRDRLAE RRLTLEVTQG AVDWLGEHGY DPIYGARPLR RLIQSSIGDL LAKALLAGRV
RDGSTVLIDL SDAKDGLTIR
//