ID A0A1K0FG63_9ACTN Unreviewed; 862 AA.
AC A0A1K0FG63;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=BG844_24345 {ECO:0000313|EMBL:OJF11789.1};
OS Couchioplanes caeruleus subsp. caeruleus.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Couchioplanes.
OX NCBI_TaxID=56427 {ECO:0000313|EMBL:OJF11789.1, ECO:0000313|Proteomes:UP000182486};
RN [1] {ECO:0000313|EMBL:OJF11789.1, ECO:0000313|Proteomes:UP000182486}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43634 {ECO:0000313|EMBL:OJF11789.1,
RC ECO:0000313|Proteomes:UP000182486};
RA Sheehan J., Caffrey P.;
RT "Couchioplanes caeruleus draft genome sequence.";
RL Submitted (SEP-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}.
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:OJF11789.1}.
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DR EMBL; MEIA01000276; OJF11789.1; -; Genomic_DNA.
DR RefSeq; WP_071807687.1; NZ_MEIA01000276.1.
DR AlphaFoldDB; A0A1K0FG63; -.
DR Proteomes; UP000182486; 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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000182486};
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; 94122 MW; 61A1D53D7625B338 CRC64;
MNAERLTTKS RDVITGAVAD ANQRGHATVE PWHLLLSLLD TGGSTAPALL RAAGANPADV
RRAAARAVEQ QPSARGASTA EPSLSREFVN AIGEAELIAK PLGDEYVSTE HLLAGLARVG
GAVGTALRDV GATEEALVAA FPSVRGGERR ITNQDPEQTY KALEKYSVDL TALAREGKID
PVIGRDAEIR RVVQVLSRRT KNNPVLIGEP GVGKTAIVEG LAQRIVAGDV PETLRDKKLV
SLDLGAMVAG AQYRGQFEER LKSVLEEIRN SNGQVVTFLD ELHTVVGAGK GEGSMDAGNM
LKPMLARGEL RMVGATTLDE YREHIEKDPA LERRFQPVVV GEPTVEDTIG ILRGLKGRYE
AHHRVQITDA ALVAAAALSD RYISDRFLPD KAIDLIDEAA SRLRMEIDSR PVELDQLQRQ
VDRMRVEKLA LEKETDPASL ARLERLERDL ADREEELTAL NARWERERGG LNRVGELKKQ
LDETRAELER AQRDADWERA SRLQYQEIPA LEREIESASA AEDEKTEPPM VKEEVGADDI
AEVIASWTGI PAGRMMEGET AKLLRMEESL QAKVVGQAEA VAAVSGAVRR ARAGVADPDR
PTGSFLFLGP TGVGKTELAK ALAGFLFDDE RAMVRIDMSE YGEKHSVARL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHPDV FDVLLQVLDD GRLTDGQGRT VDFRNAILVL
TSNLGSSVIS DFTLGEEERR EEVMATVRGH FKPEFLNRLD DIVVFHALTA QDLAAIVDIQ
LGRLRNRLAD RRLSLDVTEA AVQWLGEHGY DPIYGARPLR RLVQSAIGDS LAKALLAGEI
VDGDTVLVDL SDQKDGLRVA RA
//