ID A0A318H4T1_9BURK Unreviewed; 767 AA.
AC A0A318H4T1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:PXW98743.1};
GN ORFNames=C7444_102225 {ECO:0000313|EMBL:PXW98743.1};
OS Sphaerotilus hippei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Sphaerotilus.
OX NCBI_TaxID=744406 {ECO:0000313|EMBL:PXW98743.1, ECO:0000313|Proteomes:UP000247811};
RN [1] {ECO:0000313|EMBL:PXW98743.1, ECO:0000313|Proteomes:UP000247811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 566 {ECO:0000313|EMBL:PXW98743.1,
RC ECO:0000313|Proteomes:UP000247811};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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}.
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:PXW98743.1}.
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DR EMBL; QJJS01000002; PXW98743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318H4T1; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000247811; 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: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:PXW98743.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PXW98743.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247811};
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 COMPBIAS 146..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 84102 MW; 352C8AA8B061A757 CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA SEVLKACAAN IDDLRKNLAQ
FIKENTPTVG GTDEVDTQPT LGFQRVIQRA IMHVQSTGNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGV TRLDVVNYIA HGIKKSDPPE PSKSSEPSPA EVDKEEGEAK GTPLDQYTQN
LNQAARDGRI DPLIGREHEV ERVIQILCRR RKNNPLLVGE AGVGKTAIAE GLAWRIVQGD
VPDVLAEATV YSLDMGALLA GTKYRGDFEQ RLKGVLKQLK EHAHAVLFID EIHTLIGAGA
ASGGTLDASN LLKPALSSGQ IKCIGATTFT EYRGIFEKDA ALSRRFQKVD VVEPSVEQTV
EILKGLKSRF EEHHSVKYDV GALQAAAELS AKYINDRHLP DKAIDVIDEA GAAQRVLPKS
KQKKKITRTE VEEIVAKIAR IPPANVSTDD RGKLKSLDRD LKSVVFGQDA AIEALTGAIK
MARSGLGKPD KPIGSFLFSG PTGVGKTEVA KQLAYILGID LIRFDMSEYM ERHAVSRLIG
APPGYVGFDQ GGLLTEAVTK KPHCVLLLDE IEKAHPDVFN VLLQVMDHGT LTDNNGRKSD
FRNVIIVMTT NAGAETMNKA TIGFTTARES GDEMGDIKRM FTPEFRNRLD AIVSFRPLDE
EIILRVVDKF LLQLEGQLSE KKVEVTFTDA LRKHLGKRGF DPLMGARPMQ RLIQDTIRRA
LADELLFGRL SDGGRLTVDI DADGQVKLDI EPRKNDKSKA EPAAAAS
//