ID A0A1C6LMR2_9NEIS Unreviewed; 760 AA.
AC A0A1C6LMR2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SCK07794.1};
GN ORFNames=PSELUDRAFT_0421 {ECO:0000313|EMBL:SCK07794.1};
OS Vogesella sp. LIG4.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1192162 {ECO:0000313|EMBL:SCK07794.1, ECO:0000313|Proteomes:UP000198213};
RN [1] {ECO:0000313|EMBL:SCK07794.1, ECO:0000313|Proteomes:UP000198213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG4 {ECO:0000313|Proteomes:UP000198213};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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DR EMBL; LT607802; SCK07794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6LMR2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198213; Chromosome i.
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:SCK07794.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SCK07794.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198213};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..144
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 142..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 760 AA; 83152 MW; 42CB643078EF2222 CRC64;
MIAQELEVSL HMAFMDARRK RHEFISVEHL LLAMTDNPSA AEVLRACGAN IDQLKKQLTD
FIDEHTPTVP GDTDVETQPT LGFQRVIQRA ILHVQSSGKK EVTGANILVA IFGEKDSHAV
YYLHQQGISR LDVVNFISHG ITKQSSKPSP NSGSQDHHDS GEGEGEDGGS SPGGALENYT
LNLNQQARDG KIDPLIGREH EVERVIQILC RRRKNNPLLV GEAGVGKTAI AEGLARRIVA
GEVPEVLTRA TVYSLDMGAL LAGTKYRGDF EQRLKQVIKQ LAEDSHAILF IDEIHTLIGA
GAASGGTLDA SNLLKPALSN GGLRCIGATT YGEYRGIFEK DSALSRRFQK IDVPEPSVEQ
TIEILKGLKS RFEAHHGVKY TLAALSTAAE LSARYINDRH LPDKAIDVID EAGAAQKILP
KSRQKKVISK GEIEDIIAKI ARIPAKTISS DDRNVLKNLD RDLKSVVFGQ DKAIEALAAA
IKMSRSGLGN PQKPIGSFLF SGPTGVGKTE VAKQLAYFLG VELIRFDMSE YMERHAVSRL
IGAPPGYVGF EQGGLLTEQI NKHPYAVLLL DEIEKAHPDI FNVLLQVMDH GTLTDNNGRK
ADFRNVVIIM TTNAGAESLS KAAIGFTSSK QTGDEMADIK RLFSPEFRNR LDATIPFRML
DEVIILQVVD KFLMQLEQQL SDKKVEIHFS DKLREHLAKK GFDPLMGARP MARLIQDTIR
KALADELLFG KLAHGGEVSV DLDDEGKVAL SFGELAEAAV
//