ID A0A1P8FNY4_9PROT Unreviewed; 758 AA.
AC A0A1P8FNY4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:APV51807.1};
GN ORFNames=BWI17_20285 {ECO:0000313|EMBL:APV51807.1};
OS Betaproteobacteria bacterium GR16-43.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1904640 {ECO:0000313|EMBL:APV51807.1, ECO:0000313|Proteomes:UP000185830};
RN [1] {ECO:0000313|EMBL:APV51807.1, ECO:0000313|Proteomes:UP000185830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GR16-43 {ECO:0000313|EMBL:APV51807.1,
RC ECO:0000313|Proteomes:UP000185830};
RA Choi A.;
RT "Complete genome sequence of betaproteobacterium GR16-43, isolated from a
RT freshwater pond in South Korea.";
RL Submitted (DEC-2016) 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|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR EMBL; CP019169; APV51807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8FNY4; -.
DR STRING; 1904640.BWI17_20285; -.
DR KEGG; beba:BWI17_20285; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000185830; 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:0043335; P:protein unfolding; IEA:InterPro.
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 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; IPR013461; ClpA.
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 NCBIfam; TIGR02639; ClpA; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 1.
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.
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:APV51807.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:APV51807.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 144..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 758 AA; 82585 MW; 4D25F3F2D2EBD557 CRC64;
MIAQELEVSL HMAFVEARQK RHEFITVEHL LLALCDNPSA AEVLKACAAK IDELKKALAD
FVMQHTPTVA GTGEVDTQPT LGFQRVIQRA ILHVQSSGKK EVTGANVLVA IYGEKDSHAV
YFLHQQGVSR LDVVNYISHG ITKAPQAPGA REEGEGEQEA PEAQSGGALE SFTQNLNQLA
IDGKIDPLIG RESEIERVIQ ILCRRRKNNP LLVGEAGVGK TAIAEGLAKR VVDNQVPEIL
AKAQVYALDM GALLAGTKYR GDFEQRLKAV LKQLVDNPNA ILFIDEIHTL IGAGSASGGT
LDASNLLKPA LSSGALKCIG ATTYNEFRGI FEKDHALSRR FQKIDVNEPS IAETVDILRG
LKSRFESHHG VKYTANALTT AAELSARFIN DRHLPDKAID VIDEAGALQR ILPKSKQKKV
IGKPEIEEII AKIARIPSRN VSSDDRSALK NLDRDLKNVV FGQDKAIDAL SASIKMARSG
LGNAQKPVGS FLFSGPTGVG KTEVARQLAF IMGVELIRFD MSEYMERHAV SRLIGAPPGY
VGFDQGGLLT EAITKHPYSV LLLDEIEKAH PDIFNILLQV MDHGTLTDNN GRKADFRNVA
IIMTTNAGAE GLSKNSMGFT EDRKAGDELA EIKRMFTPEF RNRLDAVISF GALDEQVILR
VVDKFLMQLE AQLSEKKVDA LFTENLKKYL AKNGFDPQMG ARPMARLIQD TIRRALADEL
LFGKLASGGK VTIDVDKDGK VALEIANSAQ SAEPAETT
//