ID A0A1H7NRY2_9BURK Unreviewed; 954 AA.
AC A0A1H7NRY2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpC {ECO:0000313|EMBL:SEL25735.1};
GN ORFNames=SAMN05192542_10637 {ECO:0000313|EMBL:SEL25735.1};
OS Paraburkholderia caballeronis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416943 {ECO:0000313|EMBL:SEL25735.1, ECO:0000313|Proteomes:UP000199120};
RN [1] {ECO:0000313|Proteomes:UP000199120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26416 {ECO:0000313|Proteomes:UP000199120};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOAJ01000006; SEL25735.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7NRY2; -.
DR STRING; 416943.SAMN05445871_5169; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000199120; 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: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 Gene3D; 4.10.860.10; UVR domain; 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; 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 PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF145; CLPA_B PROTEASE ATP BINDING SUBUNIT-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:SEL25735.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SEL25735.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199120};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 91..234
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 60..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 503..549
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 66..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 954 AA; 104565 MW; BE9C16DE668D7B5B CRC64;
MPSSLCEICH VRPAVARVTV VQNGERRTMS ICNYDYRQLM RHQSMLNPFD SLLGGGGLSR
FFGDGGDGQP HDDEPDDAWS AEVPRESVDP TDAFSEQTME LLQRAAEKAH ELRRNELDSE
HLLYVLADTD VVVALLKELK LSPQDIQGYI DAHAQTGTAS PDASIEKMTI SPRLKKAFQF
AFQASRDLGH SYVGPEHLLI GLASVPESIA GTLLKKYGVT PEALRQKVVK VVGKGAEDGR
VDTPTGTPTL DKFGRDLTVL ARQGKLDPVL GRAQEIESTI EVLARRKKNN PVLIGEPGVG
KTAIVEGLAQ RIVNGDVPEV LRGKRLVEVN INSMVAGAKY RGEFEERAKQ LIDEVTAKHD
ELILFVDELH TIVGAGQGGG EGGLDIANVL KPALARGELS LIGATTLNEY QKYIEKDAAL
ERRFQPVLVP EPTVEQTIVI LRGLRDKLEA HHQVTFADDA FVAAAELADR YITTRFLPDK
AIDLIDQAAA RVRIGSTSRP AAIQELEAEI AQLRREQDYA SSRKRFDEAK RFEERIGDKQ
SALDEATEAW QRKTGSETLE VTVEAVAEVV SRLTGIPVTE LTQAERQKLL NMEETLRERV
VGQDDAVVAV SDAVRLSRAG LGQTHRPIAT FLFLGPTGVG KTELAKALAE VVFGDEQAII
RIDMSEYMER HAVARLIGAP PGYVGYDEGG QLTERVRRRP YSVILLDEIE KAHPDVNNVL
LQVFDDGRLT DGKGRVVDFS NTILIATSNL GSAIIMENLT RPEAARTTDK ALRDELMKVL
KGHFRPEFLN RIDEIIVFHA LSRENIRAIV QIQLDRVVRT AAAQGITLKI DASLVEHLVD
AGYQPEFGAR ELKRQVRLDV ETRLAKEILR DTLATGDTAA IAYDSDSGQV TISKIATQPD
VKEPRAASKP AKPPKSPPPD RDAIADEIAS DDIAGEAPPR SKKNGKGAGS PARK
//
