ID A0A2I8DBQ2_9BURK Unreviewed; 949 AA.
AC A0A2I8DBQ2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Clp protease ClpC {ECO:0000313|EMBL:AUT44649.1};
GN ORFNames=C2U31_00885 {ECO:0000313|EMBL:AUT44649.1};
OS Achromobacter sp. AONIH1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=1758194 {ECO:0000313|EMBL:AUT44649.1, ECO:0000313|Proteomes:UP000236176};
RN [1] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RX PubMed=29437920;
RG NISC Comparative Sequencing Program;
RA Weingarten R.A., Johnson R.C., Conlan S., Ramsburg A.M., Dekker J.P.,
RA Lau A.F., Khil P., Odom R.T., Deming C., Park M., Thomas P.J.,
RA Henderson D.K., Palmore T.N., Segre J.A., Frank K.M.;
RT "Genomic Analysis of Hospital Plumbing Reveals Diverse Reservoir of
RT Bacterial Plasmids Conferring Carbapenem Resistance.";
RL MBio 9:e02011-e02017(2018).
RN [2] {ECO:0000313|Proteomes:UP000236176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AONIH1 {ECO:0000313|Proteomes:UP000236176};
RA Segre J.A., Mullikin J.;
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}.
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DR EMBL; CP026124; AUT44649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I8DBQ2; -.
DR KEGG; achr:C2U31_00885; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000236176; 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: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; 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; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000313|EMBL:AUT44649.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000313|EMBL:AUT44649.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236176};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 109..249
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 518..571
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 893..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 949 AA; 104536 MW; 8D4C1DD96E2D663C CRC64;
MARKQCQVCG QPATVRVEAN LNGRHSTMLL CDDHYRQLVR QQKRTVSPLE ALFGSRSGLF
EDFLGSDFFR IGDDAPSMAA DTDEVVDASF GEPAPAGTGT ARRRGSGLAS RISEQSEALL
QEAARHAAEF GRAEVDTEHL LLALSDSDVV KTILGQFKIK VDDLKRQIES EAKRGDKPFE
GEIGVSPRVK DALSRAFVAS NELGHSYVGP EHFLIGLAEE GEGLAANLLR RYGLTPQALR
QQVSKVVGKG AEDGRAETPT NTPELEKYSR DLTKMAREGK LDPVIGRAQE IETTIEVLAR
RKKNNPVLIG EPGVGKTAIV EGLAQRMVAG EVPETLRDKR LVELNINAMV AGAKYRGEFE
ERVQKVLKEV TEHQGELILF IDEVHTIVGA GQGGGEGGLD VANVFKPMMA RGELNLIGAT
TLNEYQKYIE KDAALERRFQ PVMVPEPTVA QTMMILRGLR DTFEAHHKVS ISEDAIIAAA
ELSDRYITAR FLPDKAIDLL DQAAARVKLS ATARPVAVQE LESELHQLRR EQDYVASRKQ
YDKAAELGKR IEAKEAELKK LVEEWERERA SGSAEVKAEH VAQIVSRLTG IPVNELTVEE
REKLLHLEQR LHERLVGQDE AVRAVADAVR LSRAGLREGS KPVATFLFLG PTGVGKTELA
KALAESIYGD EGALLRIDMS EYGERHTVAR LVGAPPGYVG YDEGGQLTEK VRRKPYSVLL
LDEIEKAHPD VYNILLQVFD DGRLTDGKGR VVDFTNTIII ATSNLGSDII QRRLKARGAA
GEEYEKTKSE VMDVLRGHFR PEFLNRIDEI IVFHALGKEE IRHIVGLQLD RVARNAASQG
VTLTFDQTLI DHFAEEGYKP EFGARELKRL IRSELETALA REMLGGGIGK ADHASARWDD
KAERVVFERQ EPPAKPVEPE KPDAANVAET PPSDASKPAR KKKSAGGES
//
