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Database: UniProt
Entry: A0A2I6S7B1_9RHOO
LinkDB: A0A2I6S7B1_9RHOO
Original site: A0A2I6S7B1_9RHOO 
ID   A0A2I6S7B1_9RHOO        Unreviewed;       760 AA.
AC   A0A2I6S7B1;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:AUN95143.1};
GN   Name=clpA {ECO:0000313|EMBL:AUN95143.1};
GN   ORFNames=C0099_09455 {ECO:0000313|EMBL:AUN95143.1};
OS   Pseudazoarcus pumilus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Pseudazoarcus.
OX   NCBI_TaxID=2067960 {ECO:0000313|EMBL:AUN95143.1, ECO:0000313|Proteomes:UP000242205};
RN   [1] {ECO:0000313|EMBL:AUN95143.1, ECO:0000313|Proteomes:UP000242205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SY39 {ECO:0000313|EMBL:AUN95143.1,
RC   ECO:0000313|Proteomes:UP000242205};
RA   Fu G.-Y.;
RL   Submitted (JAN-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}.
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DR   EMBL; CP025682; AUN95143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I6S7B1; -.
DR   KEGG; atw:C0099_09455; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000242205; 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:AUN95143.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AUN95143.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242205};
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          143..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   760 AA;  83755 MW;  D5FCB1FFB47D75C2 CRC64;
     MIAQELEVSL HMAFVEARQK RHEFITVEHL LLALLDNPSA AEVLKACAAN IEELRRELTN
     FINEHTPRVE NVEEVDTQPT LGFQRVIQRA ILHVQSSGKK EVTGANVLVA IFGEKDSHAV
     YFLQRQKISR LDVVNFISHG IAKTPQQGSP AQGGRAEAEP EGEQEAAQSG GALENFTQNL
     NQQALIGKID PLIGREKEVE RVIQTLCRRR KNNPLLVGEA GVGKTAIAEG LARRIVEDRV
     PDILKGAQVH ALDMGALLAG TKYRGDFEQR LKAVLKQLRE ADNTILFIDE IHTLIGAGAA
     SGGTLDASNL LKPALSSGQL KCIGATTYSE FRQIFEKDHA LSRRFQKIDV VEPSVAETVE
     ILKGLKSRFE EHHNVRYSSA ALASAAELAA RYINDRHLPD KAIDVIDEAG AAQRILPKSR
     QRKTIGRVEI EEIVAKIARI PPRTVSNDDR QSLRTLERDL KNMVFGQDEA IDALAKAIKM
     SRSGLGNPQK PIGNFLFSGP TGVGKTEVAR QLAYTLGIEL VRFDMSEYME RHAVSRLIGA
     PPGYVGYDNG GLLTEAVTKK PHCVLLLDEI EKAHPDIYNI LLQVMDHGAL TDNNGRQADF
     RNVIIIMTTN AGAEAMQKTV MGFSAKRESG DEMAEIKRLF SPEFRNRLDA TISFAALDNE
     IILKVVDKFL MQLEAQLHEK KVEAHFTDEL KAWLAAEGFD PLMGARPMAR LIQDTIRSAL
     ADELLFGRLA SGGHVTIDLG ADGKVKLEFD EEEAESATTS
//
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