ID E0NFF8_PEDAC Unreviewed; 823 AA.
AC E0NFF8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=ATPase family associated with various cellular activities (AAA) {ECO:0000313|EMBL:EFL95852.1};
GN Name=clpC {ECO:0000313|EMBL:EFL95852.1};
GN ORFNames=HMPREF0623_0888 {ECO:0000313|EMBL:EFL95852.1};
OS Pediococcus acidilactici DSM 20284.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=862514 {ECO:0000313|EMBL:EFL95852.1, ECO:0000313|Proteomes:UP000004470};
RN [1] {ECO:0000313|EMBL:EFL95852.1, ECO:0000313|Proteomes:UP000004470}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20284 {ECO:0000313|EMBL:EFL95852.1,
RC ECO:0000313|Proteomes:UP000004470};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUL-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:EFL95852.1}.
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DR EMBL; AEEG01000003; EFL95852.1; -; Genomic_DNA.
DR RefSeq; WP_004166095.1; NZ_GL397067.1.
DR AlphaFoldDB; E0NFF8; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR Proteomes; UP000004470; 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:UP000004470};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 422..457
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 148..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 411..469
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 823 AA; 91608 MW; 7E864F8BD16C88B7 CRC64;
MENLFTPSAR NVLIIAQEQA KRFKHPAVGT EHLLLALTIE NNGVAHSVLE QFNVTEIDVI
EEIEQFTGYG NLRLTKNDYL PYSPKAKEIL ANAGDQARQL KAAKIGTEHI LLALIQDETI
LSSRVLLALD TDVADVRKVT LRKLGVNPAT QSRRAKQRAT TTKGTPTLDS VARDLTAMAE
AGKIDPMIGR ENELRRVIQI LSRRTKNNPV LIGEPGVGKT AIAEGLAQRI IADDVPEDMK
NKRLMMLEMG ALVAGTKYRG EFEDRLKKVI EEIRQDGKVI LFIDELHTLI GAGGAEGAID
ASNILKPALA RGELQTIGAT TLNEYQKYIE ADAALERRFA KVEVDEPTQA EAVQILQGIR
PKYEEHHKVR ITDEAIQQAV NLSARYISDR FLPDKAIDLI DEAAAKIRID AAEKQSKRET
DEDKLARLKA DKEAAIDRQD FETAAEIRKK EMKLRKKVER AAARQAEAEQ PVEYKLQETG
EDVAQIVSDW TGVPVTQMKQ SESERLVNLE KILHEHVIGQ DEAVSSVARA IRRARSGLKN
PKRPIGSFMF LGPTGVGKTE LAKTLANVMF GSEDNMIRID MSEYMERFST SRLVGSAPGY
VGYDEGGQLT EQVRRKPYSV VLFDEVEKAH PDVFNLLLQV FDDGFLTDSK GRRVDFRNTI
IIMTSNLGAT ALRDEKSVGF GAQNMADDYQ AMAAKVKEVL KQSFRPEFLN RIDETIVFHS
LTKPELHQIV KLMSKDIIRR MSAQGINMKF TPAAIDVVAE AGFDPEYGAR PIRRALQTQV
EDQLSEMLLA GQVKVGDDVT IGARNHKITF KVKDAKLVSS TSK
//
