ID   A0A3R9ZDZ7_9BURK        Unreviewed;       773 AA.
AC   A0A3R9ZDZ7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   10-FEB-2021, entry version 11.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RST56653.1};
GN   Name=clpA {ECO:0000313|EMBL:RST56653.1};
GN   ORFNames=EJI01_02155 {ECO:0000313|EMBL:RST56653.1};
OS   Variovorax sp. MHTC-1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=2495593 {ECO:0000313|EMBL:RST56653.1, ECO:0000313|Proteomes:UP000276058};
RN   [1] {ECO:0000313|EMBL:RST56653.1, ECO:0000313|Proteomes:UP000276058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MHTC-1 {ECO:0000313|EMBL:RST56653.1,
RC   ECO:0000313|Proteomes:UP000276058};
RA   Gao J., Sun J.;
RT   "The genome sequence of Variovorax sp MHTC-1.";
RL   Submitted (DEC-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:ARBA00002405}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00011230}.
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:RST56653.1}.
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DR   EMBL; RWKI01000001; RST56653.1; -; Genomic_DNA.
DR   Proteomes; UP000276058; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043335; P:protein unfolding; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
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   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; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   TIGRFAMs; TIGR02639; ClpA; 1.
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   ECO:0000313|EMBL:RST56653.1};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Hydrolase {ECO:0000313|EMBL:RST56653.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RST56653.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276058};
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          146..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  84729 MW;  53A56F852A210837 CRC64;
     MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACSAN VDDLRASLTN
     FIKDNTPQVA GTDDVDTQPT LGFQRVIQRA IMHVQSTGNG KKEVTGANVL VAIFGEKDSH
     AVYYLHQQGV TRLDVVNFIA HGIKKSDPPE AAKGSSESSS GEGEEGGGEK NEKSSPLEQF
     TQNLNQLAKE GKIDPLIGRE YEVERVIQIL CRRRKNNPLL VGEAGVGKTA IAEGLAWRIT
     QNDVPEILAE SHVYSLDMGA LLAGTKYRGD FEQRLKGVLK SLKDKPNAIL FIDEIHTLIG
     AGAASGGTLD ASNLLKPALS SGQLKCIGAT TFTEYRGIFE KDAALSRRFQ KVDVVEPTVQ
     ETVDILKGLK SRFEEHHGVK YGVAALQAAA ELSAKYINDR HLPDKAIDVI DEAGAAQRIL
     PANKRKKTIS KAEVEEIVAK IARIPPANVS NDDRGKLQNI ERDLKSVVFG QDKALEVLAS
     AVKMARSGLG REDKPIGSFL FSGPTGVGKT EAAKQLAYIM GIELIRFDMS EYMERHAVSR
     LIGAPPGYVG FDQGGLLTEA ITKKPHAVLL LDEIEKAHPD IFNVLLQVMD HGTLTDNNGR
     KADFRNVIIV MTTNAGAETM NKATIGFTNP RQAGDEMADI KRLFTPEFRN RLDATVSFKA
     LDEQIILRVV DKFLLQLETQ LAEKKVDVTF TDALRKHLAK KGFDPLMGAR PMQRLIQDTI
     RRALADELLF GRLQEGGRLT VDLDDKEEVQ LDIQPVAKKE GRAKPEAEEA ATG
//