ID A0A4V2G721_9ACTN Unreviewed; 862 AA.
AC A0A4V2G721;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=EV385_2688 {ECO:0000313|EMBL:RZU50896.1};
OS Krasilnikovia cinnamomea.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Krasilnikovia.
OX NCBI_TaxID=349313 {ECO:0000313|EMBL:RZU50896.1, ECO:0000313|Proteomes:UP000292564};
RN [1] {ECO:0000313|EMBL:RZU50896.1, ECO:0000313|Proteomes:UP000292564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45162 {ECO:0000313|EMBL:RZU50896.1,
RC ECO:0000313|Proteomes:UP000292564};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (FEB-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|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:RZU50896.1}.
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DR EMBL; SHKY01000001; RZU50896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V2G721; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000292564; 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:RZU50896.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RZU50896.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000292564};
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; 93906 MW; 4D4067AA1543502B CRC64;
MNAERLTTKS RDVITGAVAS ASTRGHASVE PWHLLLALLD TGGSTAPGLL RAVGANPAEI
RRVAARAVEQ IPSARGASIA EPSLSREFVN AIGEAELIAK PLGDEYISTE HLLAGLARVG
GAVGKALRDA GATEETLVAA FPSVRGGDRR VTTQDPEQTY QALEKYSVDL 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
VDRMRVERLA LGKETDPASV ARLERLERDL ADREEELTAL TARWERERGG LNRVGELKQK
LDEMRVELER AQRDAEWEKA SRLQYQEIPA LEQELASASE AEEEKAEPPM VKEEVGADDI
AEVISSWTGI PAGRMMEGET AKLLRMEDSL AAKVVGQREA VEAVAGAVRR ARAGVADPDR
PTGSFLFLGP TGVGKTELAK ALAGFLFDDE RAMVRIDMSE YGEKHSVARL VGAPPGYVGY
EEGGQLTEAV RRRPYSVVLL DEVEKAHPDV FDVLLQVLDD GRLTDGQGRT VDFRNAILVL
TSNLGSSVVS DFTLSDEQRR DEVMAAVRAH FKPEFLNRLD DIVVFHALTA QDLAAIVDIQ
LARLRGRLAD RRLSLRVTDA AVHWLGEHGY DPIYGARPLR RLVQSAIGDA LAKALLGGQI
VDGDTVSVDL NDAKDGLSVS RG
//