ID A0A2N7X3L1_9BURK Unreviewed; 765 AA.
AC A0A2N7X3L1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:PMS36204.1};
GN Name=clpA {ECO:0000313|EMBL:PMS36204.1};
GN ORFNames=C0Z20_15330 {ECO:0000313|EMBL:PMS36204.1};
OS Trinickia symbiotica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=863227 {ECO:0000313|EMBL:PMS36204.1, ECO:0000313|Proteomes:UP000235777};
RN [1] {ECO:0000313|EMBL:PMS36204.1, ECO:0000313|Proteomes:UP000235777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPY 581 {ECO:0000313|EMBL:PMS36204.1,
RC ECO:0000313|Proteomes:UP000235777};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
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}.
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:PMS36204.1}.
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DR EMBL; PNYC01000008; PMS36204.1; -; Genomic_DNA.
DR RefSeq; WP_018443196.1; NZ_PTIR01000004.1.
DR AlphaFoldDB; A0A2N7X3L1; -.
DR STRING; 863227.GCA_000373005_04589; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000235777; 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:PMS36204.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PMS36204.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000235777};
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 147..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 84109 MW; 6B7DB909AB8F2625 CRC64;
MIAQELEVSL HMAFMEARQA RHEFITVEHL LLALLDNPTA AEVLRACAAN IEDLRQNLRN
FIHDNTPTVP GTDDVDTQPT LGFQRVIQRA IMHVQSTSNG KKEVTGANVL VAIFGEKDSH
AVYYLQQQGV TRLDVVNFIS HGIAKTNSSD AAKAGDSNAE SEDAASQKET PLAQFTQNLN
QMAKDGRIDP LIGRESEVER VVQVLCRRRK NNPLLVGEAG VGKTAIAEGL AWRITRGEVP
DILADAQVYS LDMGALLAGT KYRGDFEQRL KTVLKELKER PHAILFIDEI HTLIGAGAAS
GGTLDASNLL KPALSSGTLK CIGATTFTEF RGIFEKDAAL SRRFQKIDVT EPTVEQTVAI
LRGLKSRFEE HHGVKYSSGA LSAAAELSAR FITDRHLPDK AIDVIDEAGA AQRILPKSKQ
KKTIGKGEIE EIISKIARVP AQSVSQDDRS KLQTLDRDLK AVVFGQDPAI DALSAAIKMA
RAGLGKTDKP IGAFLFSGPT GVGKTEVARQ LAFTLGIELT RFDMSEYMER HAVSRLIGAP
PGYVGFDQGG LLTEAVTKKP HCVLLLDEIE KAHPDIFNVL LQVMDHGTLT DNNGRKADFR
NVIIIMTTNA GAESMQKGTI GFTTRRETGD EMADIKRMFT PEFRNRLDAT ISFRALDQEI
IMRVVDKFLM QLEDQLHEKK VDAVFTDALR QHLAKNGFDP LMGARPMQRL IQDTIRRALA
DELLFGKLMN GGRVTVDVDE ADKVQLTFDE NAVPRNPNPE TVEVE
//
