ID E4KR19_9LACT Unreviewed; 819 AA.
AC E4KR19;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=ATPase family associated with various cellular activities (AAA) {ECO:0000313|EMBL:EFR30569.1};
GN Name=clpC {ECO:0000313|EMBL:EFR30569.1};
GN ORFNames=HMPREF9257_0732 {ECO:0000313|EMBL:EFR30569.1};
OS Eremococcus coleocola ACS-139-V-Col8.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Eremococcus.
OX NCBI_TaxID=908337 {ECO:0000313|EMBL:EFR30569.1, ECO:0000313|Proteomes:UP000005990};
RN [1] {ECO:0000313|EMBL:EFR30569.1, ECO:0000313|Proteomes:UP000005990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-139-V-Col8 {ECO:0000313|EMBL:EFR30569.1,
RC ECO:0000313|Proteomes:UP000005990};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) 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. 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:EFR30569.1}.
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DR EMBL; AENN01000017; EFR30569.1; -; Genomic_DNA.
DR RefSeq; WP_006418729.1; NZ_AENN01000017.1.
DR AlphaFoldDB; E4KR19; -.
DR STRING; 908337.HMPREF9257_0732; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000005990; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000005990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 2..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 428..463
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 417..470
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 152..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 91093 MW; F26350F131F10401 CRC64;
MFEELFTESA RQAMIFAAEQ AYLLRHQAVG TEHILLGLAR EEDGIAGKVL REQGATYDAL
VRELEIIQGQ TAVPRMQGEI VIPYSPRAKK IIMNASNDAK RLGAPKVGTE HLLLGMLKEE
IYATVLLKNL GIDLNDLRKK TYNMIGLDKT DRRSVNSHRR QQEKAEAQSK TPTLDAVSRD
LTELARQDKL DPVVGRDTEI KRMVQIISRR TKNNPVLVGE PGVGKTAIAE GLAERMVGGQ
VPQDIAKKRL VMLDIASLVA GTKYRGEFEE RMKKIIDELN EDSNVILFID ELHTLIGAGG
AEGAIDASNI LKPALARGEI QVVGATTLNE YQKYIEKDAA LERRFSKVQI DEPSVDESLQ
IIAGLKERYE DHHHVSISDD ALQAAVKLSV RYQSERRLPD KAIDLIDEAA AKVRIDNSVA
ESSYKALEKQ LAELSKQKES AILDRDFERA ASIRQEEQNI ETQLEAAAEK DASDDKDNRQ
VVTADDVAEV LALATGIPVQ QMKMTESKRL VHLEEELHER VIGQEEAVSS VSRAIRRAYS
GLKNPNRPIG SFLFLGPTGV GKTELAKALA SAMFGSQDNM IRVDMSEYME KHTVSRLVGA
PPGYVGYDEA GQLTEQVRQK PYSVILLDEV EKAHPDVFNI LLQVFDDGHL TDGKGRKVDF
RNTIIIMTSN MGATALRDDK SVGFGVSDVS QDHKAMQSRI MEEVKRGFRP EFINRIDEII
VFHALNKEEI RQIVKLQTKE VIARLSDMEI GARITDTAVD IIAEAGFDPE YGARPIRRAI
QKQIEDSLSE MLLKGEIELG DAITIGGRQG EININNRSK
//
