ID A0A0R2IW47_9LACO Unreviewed; 826 AA.
AC A0A0R2IW47;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Chaperone protein clpb {ECO:0000313|EMBL:KRN65988.1};
GN ORFNames=IV80_GL001547 {ECO:0000313|EMBL:KRN65988.1};
OS Pediococcus cellicola.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus.
OX NCBI_TaxID=319652 {ECO:0000313|EMBL:KRN65988.1, ECO:0000313|Proteomes:UP000051568};
RN [1] {ECO:0000313|EMBL:KRN65988.1, ECO:0000313|Proteomes:UP000051568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17757 {ECO:0000313|EMBL:KRN65988.1,
RC ECO:0000313|Proteomes:UP000051568};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {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:KRN65988.1}.
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DR EMBL; JQBR01000006; KRN65988.1; -; Genomic_DNA.
DR RefSeq; WP_057751118.1; NZ_JQBR01000006.1.
DR AlphaFoldDB; A0A0R2IW47; -.
DR STRING; 319652.IV80_GL001547; -.
DR PATRIC; fig|319652.3.peg.1567; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051568; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 4.10.860.10; UVR domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
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 InterPro; IPR001943; UVR_dom.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF193; CHAPERONE PROTEIN CLPB; 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.
DR PROSITE; PS50151; UVR; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000051568};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 425..460
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 153..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 91628 MW; 0735E461EFDC22A7 CRC64;
MDNLFTPSAK NVLAISQEQA KRFKHQAVGT EHLLLALAIE KNGIAYKVFQ QFSVTETDIV
EEIERFTGYG TLKNIGTDDY LPYSPKAKEI LALAGDEAKR LGAAKIGTEH LLLALLSDEN
ILSSRILISL DMDLSQTRKV ILRKLGVSAS AQLRQNQAQG SRGNKPKGTP TLDSVARDMT
QMARDGQIDP VIGREKEVKR VIQILSRRTK NNPVLIGEPG VGKTAIAEGL AQRIIDGHVP
SDLANKRLMM LDMGSLVAGT KYRGEFEDRL KKVIDEIHED KHIVLFIDEL HTLIGAGGAE
GAIDASNILK PALARGELQT IGATTLNEYQ KYIETDAALE RRFAKVEVDE PTPEESVQIL
RGLRDKYEQH HQVAITDDAI KQAVDLSDRY ISDRFLPDKA IDLMDEAAAK VRIDQMGKED
QKGSKSKLQQ LVDDKEAAIE AQDFEKAQKI RVKEEKLRAK LAKQQATDDG DKKPKYQLQE
TAEDVAQVVS EWTGVPLTQL QKTESERLVN LEKILHERVI GQEEAVSAVS RAIRRARSGL
KDPGRPIGSF MFLGPTGVGK TELAKALAEA MFGSEDNMIR IDMSEYMERY STSRLIGSAP
GYVGYDEGGQ LTERVRQKPY SVVLFDEVEK AHPDVFNILL QVLDDGYLTD SKGRKVDFRN
TILIMTSNLG ATALRDEKSV GFGAKDASQD YQAMAAKIRE VLKQSFRPEF LNRIDETIIF
HSLTRPQLHQ IVKLMARNIL KRVADQGMTV KITPAAIDAV AEAGFDPEYG ARPIRRAFQT
KVEDQLSELM LSGEAKIGDN ITVGARHGKI QVAVRNPKPK PKQPTA
//
