ID A0A5C8NYP2_9BURK Unreviewed; 769 AA.
AC A0A5C8NYP2;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:TXL66240.1};
GN Name=clpA {ECO:0000313|EMBL:TXL66240.1};
GN ORFNames=FHP08_09220 {ECO:0000313|EMBL:TXL66240.1};
OS Zeimonas arvi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Zeimonas.
OX NCBI_TaxID=2498847 {ECO:0000313|EMBL:TXL66240.1, ECO:0000313|Proteomes:UP000321548};
RN [1] {ECO:0000313|EMBL:TXL66240.1, ECO:0000313|Proteomes:UP000321548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-CFT501 {ECO:0000313|EMBL:TXL66240.1,
RC ECO:0000313|Proteomes:UP000321548};
RA Lin S.-Y., Tsai C.-F., Young C.-C.;
RT "Quisquiliibacterium sp. nov., isolated from a maize field.";
RL Submitted (JUN-2019) 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:TXL66240.1}.
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DR EMBL; VDUY01000003; TXL66240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5C8NYP2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000321548; 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:TXL66240.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TXL66240.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000321548};
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 143..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 84286 MW; A669810B4FE9C962 CRC64;
MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACAAN IDELRRSLTG
FIKENTPIVP GAEEIDTQPT LGFQRVIQRA IMHVQSTSNG KKEVTGANVL VAIFGEKDSH
AVYYLHQQGI TRLDVVNFIS HGITKTPQPK EPPKDEQAEG EQEAAGGQPG ALEQYTQNLN
VAAREGRIDP LIGREQEVER VIQVLCRRRK NNPLLVGEAG VGKTAIAEGL AWRITQGDVP
EILADAVVYS LDMGALLAGT KYRGDFEQRL KAVLKQLKQA ANAILFIDEI HTLIGAGSAS
GGTLDASNLL KPALSSGQLK CIGATTYNEY RGIFEKDHAL SRRFQKIDVV EPSVEQTVQI
LRGLKSRFEE HHGVRYSASA LSAAAELSAK FINDRHLPDK AIDVIDEAGA AQRILPKSKQ
KKVIGKNEIE DIVSKIARIP PASVSSDDRS KLQTLDRDLK ATVFGQDPAI DALAAAIKMS
RSGLGKPDKP IGAFLFSGPT GVGKTEVAKQ LAFILGIELI RFDMSEYMER HAVSRLIGAP
PGYVGFDQGG LLTEAISKKP HAVLLLDEIE KAHPDIFNIL LQVMDHGTLT DNNGRKADFR
NVIVIMTTNA GAADLQRRSI GFSDSREAGD EMVEIKRLFT PEFRNRLDSI ISFKALDEEI
ILRVVDKFLM QLEEQLHEKK VEAIFTDRLR KHLAAKGFDP LMGARPMQRL IQDTIRKALA
DELLFGKLTS GGRVTVDLDE SDQVVLSFAE GDPPSAGGEG EEQIEVLPA
//