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Database: UniProt
Entry: G0ACY4_COLFT
LinkDB: G0ACY4_COLFT
Original site: G0ACY4_COLFT 
ID   G0ACY4_COLFT            Unreviewed;       772 AA.
AC   G0ACY4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit clpA {ECO:0000313|EMBL:AEK63089.1};
GN   Name=clpA {ECO:0000313|EMBL:AEK63089.1};
GN   OrderedLocusNames=CFU_3265 {ECO:0000313|EMBL:AEK63089.1};
OS   Collimonas fungivorans (strain Ter331).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK63089.1, ECO:0000313|Proteomes:UP000008392};
RN   [1] {ECO:0000313|EMBL:AEK63089.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63089.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA   Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT   "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT   expression of ribosomal RNA genes by large-insert library fluorescent in
RT   situ hybridization (LIL-FISH).";
RL   Environ. Microbiol. 6:990-998(2004).
RN   [2] {ECO:0000313|EMBL:AEK63089.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63089.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA   Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT   "Genomic flank-sequencing of plasposon insertion sites for rapid
RT   identification of functional genes.";
RL   J. Microbiol. Methods 66:276-285(2006).
RN   [3] {ECO:0000313|EMBL:AEK63089.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63089.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA   Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA   Leveau J.H.;
RT   "Identification and characterization of genes underlying chitinolysis in
RT   Collimonas fungivorans Ter331.";
RL   FEMS Microbiol. Ecol. 66:123-135(2008).
RN   [4] {ECO:0000313|EMBL:AEK63089.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63089.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA   Leveau J.H., Uroz S., de Boer W.;
RT   "The bacterial genus Collimonas: mycophagy, weathering and other adaptive
RT   solutions to life in oligotrophic soil environments.";
RL   Environ. Microbiol. 12:281-292(2010).
RN   [5] {ECO:0000313|EMBL:AEK63089.1, ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|EMBL:AEK63089.1,
RC   ECO:0000313|Proteomes:UP000008392};
RX   PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA   Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA   van den Berg M., Leveau J.H.;
RT   "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT   Collimonas fungivorans versus Aspergillus niger.";
RL   ISME J. 5:1494-1504(2011).
RN   [6] {ECO:0000313|Proteomes:UP000008392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA   Leveau J.H.;
RT   "Complete sequence of Collimonas fungivorans Ter331.";
RL   Submitted (MAY-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; CP002745; AEK63089.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0ACY4; -.
DR   STRING; 1005048.CFU_3265; -.
DR   KEGG; cfu:CFU_3265; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_4; -.
DR   OMA; GRVIQEH; -.
DR   Proteomes; UP000008392; 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:AEK63089.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AEK63089.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008392};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..152
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          152..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   772 AA;  84972 MW;  E174545D31FA964F CRC64;
     MHDGGSMIAQ ELEVSLHMAF VEARQARHEF ITVEHLLLAL LDNPSAAEVL RACAVNIDDM
     RKTLTIFIGD NTPTVPGSNE VDTQPTLGFQ RVIQRAIMHV QSASNGKKEV TGANVLVAIF
     GEKDSHAVYY LHQQGVTRLD VVNFISHGVR KDQQADAQKS SEGAEEVQAE GQAKESPLDQ
     FTQNLNKLAT EGKIDPLIGR EYEVERVIQT LCRRRKNNPL LVGEAGVGKT AIAEGLAWRI
     TQGDVPEILQ NAIVYSLDMG SLLAGTKYRG DFEQRLKAVL KQLKDSPNGI LFIDEIHTII
     GAGSASGGTL DASNLLKPAL SSGQLKCIGA TTYTEFRGVF EKDHALSRRF QKIDVNEPTV
     EQTVQILRGL KSRFEEHHGV KYSASALTSA AELAARFIND RHLPDKAIDV IDEAGAAQRI
     LPKSKQKKTI GKGEIEDIIA KIARIPPQSV NQDDRSKLQT IDRDLRNVVF GQDPAIDALA
     SAIKMARAGL GKTDRPIGSF LFSGPTGVGK TEVAKQLAFI LGIDLIRFDM SEYMERHAVS
     RLIGAPPGYV GFDQGGLLTE AVTKKPHAVL LLDEIEKAHP DIFNILLQVM DHGALTDNNG
     RKADFRNVII IMTTNAGAES LQKRSIGFTD KKEAGDEMAD IKRMFTPEFR NRIDSIISFH
     ALDEEVILRV VDKFLMQLEE QLHEKKVEAV FTENLRKFLA KKGFDPLMGA RPMSRLIQDM
     IRKALADELL FGKLVTGGRV TVDLDDKDLI SLDFAEKDSS SPAAPEETVE VE
//
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