ID H5WV60_9BURK Unreviewed; 767 AA.
AC H5WV60;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpA {ECO:0000313|EMBL:EHR72267.1};
GN ORFNames=BurJ1DRAFT_3459 {ECO:0000313|EMBL:EHR72267.1};
OS Burkholderiales bacterium JOSHI_001.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR72267.1, ECO:0000313|Proteomes:UP000004674};
RN [1] {ECO:0000313|EMBL:EHR72267.1, ECO:0000313|Proteomes:UP000004674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR72267.1,
RC ECO:0000313|Proteomes:UP000004674};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Smith J., Lewis G.,
RA Woyke T.;
RT "Noncontiguous Finished sequence of Burkholderiales bacterium JOSHI_001.";
RL Submitted (NOV-2011) 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; CM001438; EHR72267.1; -; Genomic_DNA.
DR AlphaFoldDB; H5WV60; -.
DR STRING; 864051.BurJ1DRAFT_3459; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_4; -.
DR OrthoDB; 9803641at2; -.
DR BioCyc; BBAC864051:G1H30-3447-MONOMER; -.
DR Proteomes; UP000004674; 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:EHR72267.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:EHR72267.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004674};
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 REGION 143..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 84075 MW; E71F96055A725745 CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACAAN IDDLRKSLAT
FIKENTPTVG GSEEVDTQPT LGFQRVIQRA IMHVQSTGSG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNFIA HGIKKSDPPE PTKGNEGGAE GEKEEGGGDG KGSPLDQFTQ
NLNQLARDGK IDPLIGRDAE VERVIQVLCR RRKNNPLLVG EAGVGKTAIA EGLAWRITQN
DVPEVLAQST VFALDMGALL AGTKYRGDFE QRLKGVLKQL KEQPSAILFI DEIHTLIGAG
AASGGTLDAS NLLKPALSNG SMKCIGATTF TEYRGIFEKD AALSRRFQKV DVVEPTVEQT
VEILKGLKSR FEDHHSVKYA VAALQAAAEL SAKYINDRHL PDKAIDVIDE AGAAQRILPS
NKRKKTITRA EVEDIVAKIA RIPPQSVSSD DRSKLKTLDR DLKSVVFGQD PAIEALAAAI
KMARSGLGKP DKPIGSFLFS GPTGVGKTEV AKQLAYILGI ELIRFDMSEY MERHAVSRLI
GAPPGYVGFD QGGLLTEAVT KKPHAVLLMD EIEKAHPDVF NVLLQVMDHG TLTDNNGRKA
DFRNVIIVMT TNAGAETMNK STIGFTTRRE QGDEMGDIKR LFTPEFRNRL DAVVSFRALD
EEIILRVVDK FLLQLESQLT EKKVEVTFTD ALRKHLAKKG FDPLMGARPM QRLIQDMIRR
ALADELLFGR LTDGGRLTVD INDKDEVQLD IQPPKKSDKP KAETTSV
//
