ID C2EQT9_9LACO Unreviewed; 828 AA.
AC C2EQT9;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=ATPase family associated with various cellular activities (AAA) {ECO:0000313|EMBL:EEJ71092.1};
GN Name=clpC {ECO:0000313|EMBL:EEJ71092.1};
GN ORFNames=HMPREF0548_2035 {ECO:0000313|EMBL:EEJ71092.1};
OS Lactobacillus ultunensis DSM 16047.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=525365 {ECO:0000313|EMBL:EEJ71092.1, ECO:0000313|Proteomes:UP000005583};
RN [1] {ECO:0000313|EMBL:EEJ71092.1, ECO:0000313|Proteomes:UP000005583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16047 {ECO:0000313|EMBL:EEJ71092.1,
RC ECO:0000313|Proteomes:UP000005583};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) 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:EEJ71092.1}.
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DR EMBL; ACGU01000110; EEJ71092.1; -; Genomic_DNA.
DR RefSeq; WP_007126792.1; NZ_GG693256.1.
DR AlphaFoldDB; C2EQT9; -.
DR STRING; 525365.HMPREF0548_2035; -.
DR PATRIC; fig|525365.8.peg.1156; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000005583; 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 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 431..466
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 150..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 427..473
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 828 AA; 92162 MW; 4276FEFEA5FD1CAE CRC64;
MENSYSKSVN QVLEIAREQA QNFHHRLIGT EHVLLALVIE TDGEAGKILR SWGLTPTAIR
EEIERYTGYG SAPKASYMEM SPRLSLALDY AKRQADQGGY KEIQTNHVLL GITASEQVLS
AMILKNLNVD IARLRQDAID SLEQDQDFGD SANWLGNNNT AAPAQKKRKT STTPTLDKVA
VNLNQRVREG GIDPVIGREK EIKRVIQILS RRTKNNPVLV GEPGVGKTAV AEAIATEIVK
KKVPEDLMNK RVMALNMGSL VAGTKYRGEF EDRMKKILDE IAKDGKVILF VDEMHTLIGA
GGAEGAIDAS NILKPSLARG DIQMIGATTF DEYQKYIEKD QALARRFQQV RLNEPSRKDA
LAILQGLKPR YEKFHHVTIS EASLEDAVDL SSRYISDRFL PDKAIDLVDE ASAAVKIRNN
IGSSKELVQI NDQIKKLIDQ KNEAAASQNF VKAAQLQDEQ NNLQARREKL VDTLHTKVSA
DATVEPEDIA KVVSDWTGVP VTQMKRNETR QLANLESILH KRVIGQDKAV SAVARAIRRS
RSGIKDERRP IGSFLFLGPT GVGKTELAKS VAAAMFGSED NLIRLDMSEY MDQIASSKLI
GSAPGYVGYE EGGQLSEQVR RHPYSVVLLD EVEKAHPDVF NLLLQVLDEG FLTDSKGRKV
DFRNTIIIMT SNLGSRSLFD SNAVGFNADK VDPSKARQAK VEQAIKQFFR PEFLNRIDET
IVFDELTKKQ LRNIVTLLTH KLVVRLQKKG ITLKLSRAAL DKIVKDGYDP ENGARPLRRA
IQNDIEDKVA EMLITGEVKK GDTLKIGSQR GHLKFEVVHS KKKLEKVK
//
