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Database: UniProt
Entry: A0A1C6LMR2_9NEIS
LinkDB: A0A1C6LMR2_9NEIS
Original site: A0A1C6LMR2_9NEIS 
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
//
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