ID D5H152_LACCS Unreviewed; 826 AA.
AC D5H152;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=ATPase AAA-2 domain protein {ECO:0000313|EMBL:CBL49737.1};
GN Name=clpC {ECO:0000313|EMBL:CBL49737.1};
GN OrderedLocusNames=LCRIS_00290 {ECO:0000313|EMBL:CBL49737.1};
OS Lactobacillus crispatus (strain ST1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=748671 {ECO:0000313|EMBL:CBL49737.1, ECO:0000313|Proteomes:UP000002371};
RN [1] {ECO:0000313|EMBL:CBL49737.1, ECO:0000313|Proteomes:UP000002371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST1 {ECO:0000313|EMBL:CBL49737.1,
RC ECO:0000313|Proteomes:UP000002371};
RX PubMed=20435723; DOI=10.1128/JB.00399-10;
RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA Edelman S., Westerlund-Wikstrom B., Korhonen T.K., Paulin L., Kankainen M.;
RT "Genome sequence of Lactobacillus crispatus ST1.";
RL J. Bacteriol. 192:3547-3548(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ST1;
RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA Edelman S., Westerlund-Wikstroem B., Korhonen T.K., Paulin L.,
RA Kankainen M.;
RT "Genome Sequence of Lactobacillus crispatus ST1.";
RL Submitted (MAR-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}.
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DR EMBL; FN692037; CBL49737.1; -; Genomic_DNA.
DR RefSeq; WP_013085811.1; NC_014106.1.
DR AlphaFoldDB; D5H152; -.
DR KEGG; lcr:LCRIS_00290; -.
DR PATRIC; fig|748671.3.peg.282; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR Proteomes; UP000002371; 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 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 429..464
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 140..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 425..474
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 826 AA; 92126 MW; 016B32EC1DF524C5 CRC64;
MENSYSKSVN QVLKIAREQA QNFHHRLIGT EHVLLALVIE TDGEAGKILR SWGLTPTAVR
EEIERYTGYG SAPKTSYMEM SPRLSLALDY ARRRANDDGV KEINTNHVLL GITASEQVLS
AMILKNLNVD IPRLQQDVED SLSQDQDFGD SANWLGDDNT TTGQKKRKST TPNLDKVAVN
LNQRVRNGEI DPVIGRDQEI KRVIQILSRR TKNNPVLVGE PGVGKTAVAE AIATEIVNKK
VPQDMLKKRV MALNLGSLVA GTKYRGEFED RMKKILNEVT KDGNVILFVD EMHTLIGAGG
AEGAIDASNI LKPSLARGDI QMIGATTFNE YQKYIEKDQA LARRFQQVRL SEPSRDDTLT
IMRGLKSKYE KFHHVTISDE SLKDAVDLST RYISDRFLPD KAIDLVDEAG AAVKIRNNVG
NDAKLEKINE QIKEIIAQKN EAAASQNFVK AAQLQDQQNN LQMQREAMVE KLEDKVSAKA
VVEPEDIAKV VSEWTGVPVT QMKRNESRQL ANLEKILHQR VIGQDKAVSA VARAIRRSRS
GIKDERRPIG SFLFLGPTGV GKTELAKSVA AAMFGSEDNL VRLDMSEYMD QIASSKLIGS
APGYVGYEEG GQLSEKVRRH PYSVILLDEV EKAHPDVFNL LLQVLDEGFL TDSKGRKVDF
RNTIIIMTSN LGSRSLFDNK AVGFNADNVD PAKARSAKVE QAIKQFFRPE FLNRIDETII
FDELDKKQLR NIVTLLTHKL VVRLQKKGIE LKLSRAALDQ IAQDGYDPEN GARPLRRAIQ
NDIEDKIAEM LIVGEIKSGD TLKIGSQHGH LKFEVVNPKK ETVKVK
//
