ID A0A511AWW5_9LACT Unreviewed; 831 AA.
AC A0A511AWW5;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:GEK92132.1};
GN Name=clpC {ECO:0000313|EMBL:GEK92132.1};
GN ORFNames=AKA01nite_17540 {ECO:0000313|EMBL:GEK92132.1};
OS Alkalibacterium kapii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=426704 {ECO:0000313|EMBL:GEK92132.1, ECO:0000313|Proteomes:UP000321662};
RN [1] {ECO:0000313|EMBL:GEK92132.1, ECO:0000313|Proteomes:UP000321662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103247 {ECO:0000313|EMBL:GEK92132.1,
RC ECO:0000313|Proteomes:UP000321662};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Alkalibacterium kapii NBRC 103247.";
RL Submitted (JUL-2019) 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:GEK92132.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BJUY01000034; GEK92132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A511AWW5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000321662; Unassembled WGS sequence.
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:SF18; HEAT SHOCK PROTEIN 104; 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 Hydrolase {ECO:0000313|EMBL:GEK92132.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:GEK92132.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000321662};
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 DOMAIN 429..464
FT /note="UVR"
FT /evidence="ECO:0000259|PROSITE:PS50151"
FT REGION 151..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 93193 MW; 5C7DD31534870FD5 CRC64;
MNELFTDKAK KALLIAQEEA KSFRHSTVGT EHLLLGLVIE NEGIAGKTLR DLGINEEDVK
DEIEHFSIYG SSQFVPKQAI LPYSPRARQI IKYATDEARR MKRPLVGTEH LLLGLLRDEN
ILSAKILNNL DVNLAKARQL VLKKLGTKMN SAKSKLNNRR PVKGNQESPN GTPTLDSLAR
DLTQQARENR LDPIVGRNKE VRRIIQILSR RTKNNPVLVG EPGVGKTAIA EGLAQKIISG
EVPPVLADKR LMTLDMGSLV AGTKYRGEFE ERMKKIIDEI YHDGKVILFI DELHTLIGAG
GAEGAIDASN ILKPALARGE LQTIGATTLD EYQKHIEKDA ALERRFASIH VDPPTEIEAE
EILFGLRKRY EDHHDVKITD AAIRAAVQFS VRYITSRQLP DKAIDLMDES ASKIRMDNSD
TPTTLSKETE KLEDLVKQKE EAIQSQDFER AARIREKEMR QRRKLEKIIK KDEQGTNDQL
EVTASDIAEV VSQWTGIPVN QMEQKESERL LKLEEVLHQR VVGQEEAVVA VSKAIRRARS
GLKDPNRPIG SFMFLGPTGV GKTELAKALA EAMFGSEEAL IRVDMSEFME KYSTSRLVGS
PPGYVGYDEG GQLTEKIRQK PYSVILLDEV EKAHPDVFNI LLQVLDDGLL TDGKGRKVDF
KNTIMIMTSN LGATALRDEK SVGFGAVDKR FDHDAMEKRI REELRNAFRP EFLNRVDDTI
VFHSLKKEEL REIVQLLTKN VIERINELGI ELKITRAAMD VIAEEGFDPE YGARPLKRAI
QNKFEDRLSE ALLAGEISFG DKVTLGATKG EITLKVRESK KTNKSQSVAN K
//