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Database: UniProt
Entry: A0A318H4T1_9BURK
LinkDB: A0A318H4T1_9BURK
Original site: A0A318H4T1_9BURK 
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
//
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