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Database: UniProt
Entry: A0A239ST19_9BURK
LinkDB: A0A239ST19_9BURK
Original site: A0A239ST19_9BURK 
ID   A0A239ST19_9BURK        Unreviewed;       765 AA.
AC   A0A239ST19;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-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:SNU87884.1};
GN   Name=clpA {ECO:0000313|EMBL:SNU87884.1};
GN   ORFNames=SAMEA4530655_04000 {ECO:0000313|EMBL:SNU87884.1};
OS   Pandoraea sputorum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Pandoraea.
OX   NCBI_TaxID=93222 {ECO:0000313|EMBL:SNU87884.1, ECO:0000313|Proteomes:UP000215126};
RN   [1] {ECO:0000313|EMBL:SNU87884.1, ECO:0000313|Proteomes:UP000215126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13161 {ECO:0000313|EMBL:SNU87884.1,
RC   ECO:0000313|Proteomes:UP000215126};
RG   Pathogen Informatics;
RL   Submitted (JUN-2017) 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; LT906435; SNU87884.1; -; Genomic_DNA.
DR   RefSeq; WP_039400867.1; NZ_LT906435.1.
DR   AlphaFoldDB; A0A239ST19; -.
DR   STRING; 93222.NA29_24065; -.
DR   KEGG; pspu:NA29_24065; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000215126; Chromosome 1.
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:SNU87884.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SNU87884.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REGION          146..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   765 AA;  83853 MW;  3811029D0D52D6B4 CRC64;
     MIAQELEVSL HMAFMEARQA RHEFITVEHL LLALLDNPTA AEVLRACAAN LDDLRQNLRN
     FIADNTPTVP GSDEVDTQPT LGFQRVIQRA IMHVQSTSNG KKEVTGANVL VAIFGEKDSH
     AVYYLQQQGV TRLDVVNFIS HGITKTGASG ESAKAGEGSA EGEEGANAKE SPLAQYTQNL
     NQMARDGKID PLIGRESEVE RVVQVLCRRR KNNPLLVGEA GVGKTAIAEG LAWRVTRGEV
     PEILQDATVY SLDMGALLAG TKYRGDFEQR LKAVLKELKE RNNAILFIDE IHTLIGAGAA
     SGGTLDASNL LKPALSSGQL KCIGATTFTE YRGIFEKDAA LSRRFQKIDV NEPTVEQTVQ
     ILRGLKSRFE EHHGVKYSSS ALSAAAELSA KFITDRHLPD KAIDVIDEAG AAQRILPKSK
     QKKTIGKGEI EEIVSKIARI PAQSVSADDR GKLQTLDRDL KSVVFGQDPA IDALSAAIKM
     SRAGLGKTDK PIGAFLFSGP TGVGKTEVAK QLAFTLGIEL IRFDMSEYME RHAVSRLIGA
     PPGYVGFDQG GLLTEAVTKK PHCVLLLDEI EKAHPDIFNV LLQVMDHGTL TDNNGRKADF
     RNVIIIMTTN AGAETINRAS IGFTNERQAG DEMADIKRMF TPEFRNRLDS IISFKPLDEQ
     IILRVVDKFL IQLEDQLHEK KVEVVFTDKL RAYLSKKGFD PLMGARPMQR LIQDTIRRAL
     ADELLFGRLT SGGRVTVDLD ENDQVQLSFP EDGNTKAQPE AAEVE
//
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