ID B1MW25_LEUCK Unreviewed; 821 AA.
AC B1MW25;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=ATPase with chaperone activity, ATP-binding subunit {ECO:0000313|EMBL:ACA83429.1};
GN Name=clpC {ECO:0000313|EMBL:ACA83429.1};
GN OrderedLocusNames=LCK_01606 {ECO:0000313|EMBL:ACA83429.1};
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519 {ECO:0000313|EMBL:ACA83429.1, ECO:0000313|Proteomes:UP000002166};
RN [1] {ECO:0000313|EMBL:ACA83429.1, ECO:0000313|Proteomes:UP000002166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20 {ECO:0000313|EMBL:ACA83429.1,
RC ECO:0000313|Proteomes:UP000002166};
RX PubMed=18281406; DOI=10.1128/JB.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
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}.
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DR EMBL; DQ489736; ACA83429.1; -; Genomic_DNA.
DR RefSeq; WP_004909195.1; NC_010471.1.
DR AlphaFoldDB; B1MW25; -.
DR STRING; 349519.LCK_01606; -.
DR GeneID; 61103230; -.
DR KEGG; lci:LCK_01606; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000002166; Chromosome.
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 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.
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 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 REGION 152..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 444..471
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 159..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 90924 MW; 03268DA15E500119 CRC64;
MDNKYTSSAQ NVLVLAQEQA KYFKHQAVGT EHLLLALAIE KEGIASKILG QFNVTDDDIR
EEIEHFTGYG MTSRYDKNVY LPYSPKAGDI LRQSGEESRA LAQTQVGTEH VLLALLQDES
ILSSRILLAL DANLQEMRRA ILRKLGVTDV RKQMKQRDKQ QSQGTPTLDS LARNLTQRAK
DNKMDPIIGR SKEVRRVVQI LSRRTKNNPV LIGEPGVGKT AIAEGLAQRI IANDVPDTLK
NKRLMALDMG SLVAGTKYRG EFEDRLKKII EEIYQDGQVI LFIDELHTLI GAGGAEGAID
ASNILKPALA RGELQTLGAT TFDEYQKYVE SDAALERRFA PVTVDEPSQE DAISILKGIR
SKFESHHQVA IDDAAIIAAV KLSSRYITDR FLPDKAIDLM DEAGAKVRID AINRPNPVNK
NKAKLAETVA AKEAAITALD FEGAAKLRTE EVRLKKRINK AEAKLADDTQ QNYHLHVTEE
DIAEVISQQT GVPLTQLEKN EQQRLVNLEA VLGRRVIGQK AAISAVARAI RRARSGLKDP
NRPIGTFMFL GPTGVGKTEL AKALAEAMFG SQENMIRIDM SEYQERWSAS RLVGSAPGYV
GYDEGGQLTE QVRNHPYSVV LLDEAEKAHQ DIFNLMLQVF DDGFLTDSKG RKVDFRNTII
IMTSNLGATR LRDEKSVGFG AVDLKNNHAA MAEKIRETLK ETFRPEFINR LDEAVVFEPL
TKDELHQIVK LMSRTVLQRV AEQGISVKIT PAAIDVVASA GFDPEYGARP IRRALQTKIE
DVLSEELLRG QITTDTTVTI GAKNGDIRLS IKPIDKVAAK A
//
