ID C9ACW7_ENTCA Unreviewed; 826 AA.
AC C9ACW7;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:EEV40726.2};
GN ORFNames=ECBG_02995 {ECO:0000313|EMBL:EEV40726.2};
OS Enterococcus casseliflavus EC20.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=565655 {ECO:0000313|EMBL:EEV40726.2, ECO:0000313|Proteomes:UP000012675};
RN [1] {ECO:0000313|EMBL:EEV40726.2, ECO:0000313|Proteomes:UP000012675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC20 {ECO:0000313|EMBL:EEV40726.2,
RC ECO:0000313|Proteomes:UP000012675};
RG The Broad Institute Genome Sequencing Platform;
RA Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K.,
RA Lander E., Nusbaum C., Galagan J., Birren B.;
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEV40726.2, ECO:0000313|Proteomes:UP000012675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC20 {ECO:0000313|EMBL:EEV40726.2,
RC ECO:0000313|Proteomes:UP000012675};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Russ C., Feldgarden M., Gilmore M., Manson J., Palmer K., Carniol K.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus casseliflavus EC20 (899205).";
RL Submitted (MAR-2013) 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; CP004856; EEV40726.2; -; Genomic_DNA.
DR RefSeq; WP_010748867.1; NZ_AKCC01000001.1.
DR AlphaFoldDB; C9ACW7; -.
DR GeneID; 15143710; -.
DR KEGG; ecas:ECBG_02995; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_9; -.
DR Proteomes; UP000012675; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:EEV40726.2};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EEV40726.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000012675};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..148
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 427..462
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 145..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 409..443
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 826 AA; 91969 MW; 4FF4450BB09DD90B CRC64;
MDELFTQRAK AVLAIAQEEA KYFKHQAVGS EHILLALVIE QNGIAGKTLR EMNITENDIR
EEIEHLTGYG TVRQYPENAY LAYSPRAKHT FAYAGDEAKR LGAPQIGTEH LLLGLLRDED
ILASRIMLNL GLSLAKMRQL LKKKMGFNES KTNGSAGRRR PAQAKAQQGT PTLDSLARDL
TKLAREKRLD PVVGRAKEVK RLIQILSRRT KNNPVLVGEP GVGKTAIAEG LAQKIINGEV
PEDMQNKRLM MLDMGALVAG TKYRGEFEDR MKKIIDEIYQ DGQIILFIDE LHTLIGAGGA
EGAIDASNIL KPALARGELQ TIGATTLDEY QKYIEKDSAL ERRFARVQVD EPTPEEAEEI
LRGLRPRYEE HHGVEISDDA LHAAVQLSVR YINSRQLPDK AIDLMDESAA KVRLDKTDES
SELADLQNEI ANLIEEKEAA IRQQDFEAAA RLRIKEKKLT QQLTEVAFME VKEASGYADS
VTAEDVATVV SQWTGVPLQQ MEKKESERLL DLEKILHQRV VGQEEAVKAV ARSIRRARSG
LKDPNRPIGS FMFLGPTGVG KTELAKALAE AMFGSEDALV RVDMSEFMEK YSTSRLIGSP
PGYVGYDEGG QLTEKIRSKP YSVILLDEVE KAHPDVFNIL LQVLDDGHLT DAKGRKVDFR
NTILIMTSNI GAQQIREEKS VGFNVTDLTK DHQAMQKRIL EELKKAFRPE FLNRVDETVV
FQSLGEGEIH EIVKIMSKAI IKRLSNQDIQ LKITPSAIDV IGKAGFDPEY GARPIRRALQ
KEVEDRLSEA LLSGQIHLGD KVTIGASKGS ITLNVKEGQA RVLQQV
//
