ID A0A0R1ZIE5_9LACO Unreviewed; 831 AA.
AC A0A0R1ZIE5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Clp protease DnaK DnaJ chaperone ATP-binding subunit {ECO:0000313|EMBL:KRM54181.1};
GN ORFNames=FC18_GL000399 {ECO:0000313|EMBL:KRM54181.1};
OS Lacticaseibacillus sharpeae JCM 1186 = DSM 20505.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1291052 {ECO:0000313|EMBL:KRM54181.1, ECO:0000313|Proteomes:UP000051679};
RN [1] {ECO:0000313|EMBL:KRM54181.1, ECO:0000313|Proteomes:UP000051679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20505 {ECO:0000313|EMBL:KRM54181.1,
RC ECO:0000313|Proteomes:UP000051679};
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:KRM54181.1}.
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DR EMBL; AYYO01000056; KRM54181.1; -; Genomic_DNA.
DR RefSeq; WP_054675416.1; NZ_BBAC01000001.1.
DR AlphaFoldDB; A0A0R1ZIE5; -.
DR STRING; 1291052.FC18_GL000399; -.
DR PATRIC; fig|1291052.5.peg.409; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051679; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 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 Hydrolase {ECO:0000313|EMBL:KRM54181.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KRM54181.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051679};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 151..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 91082 MW; EB5469B3BC6E5AAC CRC64;
MDNLFTVSAK NVLSIAQNEA RSFHHHAVGT EHILLALVTE TDGLAGKTLR QLGVTVDTVH
DDIETYTGFG SLPASAMGAD AYLPYSPKGK ALLAFAGDEA KRTGATKIGT EHILLGLLSD
EQTIAVRILA SYELTVKKLR QLVLKKMGVS DKPSARPTRQ IGTSPTPTLD GLARDLTQMA
RENKMDPVVG RDEEVARLIQ ILARRTKNNP VLIGEPGVGK TAIAEGFAER IVAGKVPMDM
RTKRVMMLDM GSLVAGTKYR GEFEDRLKKI IDEIYKNGDV ILFIDELHTL IGAGGAEGAI
DASNILKPAL ARGELQLIGA TTLDEYQKYV EKDAALERRF ATIQVNEPSQ QEAEQILRGL
RPRYEEHHGI TISDEALHAA VELSIRYITT RFLPDKAIDL VDESAAKVRI AAADKPTPTD
KLEDKIVAVT SAKETAIAAQ EFEKAATLRE DEQRLTRELA AKQANSTDDL SVRKDVVVTA
TDVAEVVAQW TGVPVTQLTK RESERLMHLE KQLHQRVVGQ EEAVSAVARA IRRARSGLKA
PNRPIGSFMF LGPTGVGKTE LAKALAESMF GSEDAIIRVD MSEYMEKYST SRLIGAAPGY
VGYEEGGQLT EKVRNKPYSV VLLDEVEKAH PDVFNLLLQV LDDGYLRDAK GRMVDFRNTI
LIMTSNLGAT ALRDEKSVGF GAKTNADDYN AMRGRILEEL KRYFRPEFLN RIDETLVFHS
LGKTELRSIV KIMAKQLLGR VREQGIGVKL TPAALDAIAK AGFDPEYGAR PIRRALQRDV
EDQLSEILLA GTAKPGDTIT IGAKKGKITF TTHHPEQATP EAKEAELTTA K
//