ID A0A0R2ET57_9LACO Unreviewed; 821 AA.
AC A0A0R2ET57;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ATP-dependent Clp protease ATP-binding protein ClpC {ECO:0000313|EMBL:KRN18347.1};
GN ORFNames=FC75_GL000755 {ECO:0000313|EMBL:KRN18347.1};
OS Lacticaseibacillus camelliae DSM 22697 = JCM 13995.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1423730 {ECO:0000313|EMBL:KRN18347.1, ECO:0000313|Proteomes:UP000050865};
RN [1] {ECO:0000313|EMBL:KRN18347.1, ECO:0000313|Proteomes:UP000050865}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22697 {ECO:0000313|EMBL:KRN18347.1,
RC ECO:0000313|Proteomes:UP000050865};
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:KRN18347.1}.
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DR EMBL; AYZJ01000093; KRN18347.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2ET57; -.
DR STRING; 1423730.FC75_GL000755; -.
DR PATRIC; fig|1423730.4.peg.789; -.
DR Proteomes; UP000050865; 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; -; 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; 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: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.
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 Hydrolase {ECO:0000313|EMBL:KRN18347.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KRN18347.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050865};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..137
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 417..452
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 90430 MW; 870F42269A26EA5F CRC64;
MIAQEQAKYF HHHAVGTEHL LMALVMEQEG IAGKTLRQLG ISEQDIHDEI ERFTGYGTVD
EGSQSKDAYL PYSPKGKEIL SYAGDEAKRL GALKIGTEHI LLGLLREDDI LAARILQDLD
LSLSKTRQLV LKKMGISDAA AKHRGAAGAQ RGGRPASQGT PTLDGLARDL TQLARENRMD
PVVGRDKEVR RLIQILARRT KNNPVLIGEP GVGKTAIAEG FAEKIVAGEV PDDMKNKRLM
ALDMGSLVAG TKYRGEFEDR LKKVIDEIYQ DGNVILFVDE LHTLIGAGGA EGAIDASNIL
KPSLARGELQ LIGATTLDEY QKYIEKDAAL ERRFATITVE EPSEAEAEEI LKGLRPRYEA
HHGVTITDEA LHEAVSLSSR YISGRFLPDK AIDLMDESAA KVRLDEADRP TKADKLQKQL
KETVKAKDDA IMHQDFETAA TIREKEQKLR TKIDAAPEPV DANGVRTDVK VGPEDVAEVV
SQWTGVPVTQ LQKKESERLI NLEKVLHERV VGQDEAVSAV ARAIRRARSG LKDPTRPIGS
FMFLGPTGVG KTELAKALAE AMFGSEDAMI RVDMSEYMEK YSTSRLIGAA PGYVGYDEGG
QLTEQVRNKP YSVVLLDEVE KAHPDVFNIL LQVLDDGFLT DSKGRRVDFR NTILIMTSNI
GATSLRDDKA VGFGKGSPTQ DFKSMQSRML EELKKAFRPE FLNRIDETVV FHSLTEKELH
EIVKIMTKQV LHRLSDQDIT VKITAAGINA VAKAGFDPEY GARPIRRALQ RDVEDQLSEL
LLTGQAGAGD TITIGARKGK LTFHIKKGQQ PVQAKKEPVH A
//