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Database: UniProt
Entry: A0A3E1RIM9_9BURK
LinkDB: A0A3E1RIM9_9BURK
Original site: A0A3E1RIM9_9BURK 
ID   A0A3E1RIM9_9BURK        Unreviewed;       773 AA.
AC   A0A3E1RIM9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:RFO98852.1};
GN   Name=clpA {ECO:0000313|EMBL:RFO98852.1};
GN   ORFNames=DIC66_02995 {ECO:0000313|EMBL:RFO98852.1};
OS   Rhodoferax lacus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=2184758 {ECO:0000313|EMBL:RFO98852.1, ECO:0000313|Proteomes:UP000260665};
RN   [1] {ECO:0000313|EMBL:RFO98852.1, ECO:0000313|Proteomes:UP000260665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC26218 {ECO:0000313|EMBL:RFO98852.1,
RC   ECO:0000313|Proteomes:UP000260665};
RA   Park M.;
RT   "Rhodoferax soyangensis sp.nov., isolated from an oligotrophic freshwater
RT   lake.";
RL   Submitted (MAY-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, 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:RFO98852.1}.
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DR   EMBL; QFZK01000001; RFO98852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E1RIM9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000260665; 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:RFO98852.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:RFO98852.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000260665};
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          146..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          752..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        146..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  84848 MW;  819A7D1ADC210BBF CRC64;
     MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACSAN IDDLRKSLAN
     FIKDNTPQVA GTDEVDTQPT LGFQRVIQRA IMHVQSTGSG KKEVTGANVL VAIFGEKDSH
     AVYYLHQQGV TRLDVVNFIA HGIKKNDPPE AAKSSEAPNE AEEGGAEKNE KSSPLEQYTV
     NLNQLAKDGK IDPLIGREYE VERVIQILCR RRKNNPLLVG EAGVGKTAIA EGLAWRITQN
     DVPEILAEAV VYSLDMGALL AGTKYRGDFE QRLKGVLKSL KDKPNGILFI DEIHTLIGAG
     AASGGTLDAS NLLKPGLSSG QLKCIGATTF TEYRGIFEKD AALSRRFQKV DVVEPTVEQT
     VEILKGLKSR FEEHHGVKYA VAALQAAAEL SAKYINDRHL PDKAIDVIDE AGAAQRILPP
     SKRKKTISKT EVEEIVAKIA RIPAANVSND DRGKLKTLER DLRNVVFGQD KAIDVLASAV
     KMARSGLGKG DKPIGSFLFS GPTGVGKTEA AKQLAYIMGI DLIRFDMSEY MERHAVSRLI
     GAPPGYVGFD QGGLLTEAVT KKPHCVLLLD EIEKAHPDIF NVLLQVMDHG TLTDNNGRKA
     DFRNVIIIMT TNAGAETMNK ATIGFTNPRE SGDEMADIKR LFTPEFRNRL DALVSFKALD
     ENIILRVVDK FLLQLETQLA EKKVDVTFTD KLRKHLGKKG FDPLMGARPM QRLIQDTIRR
     ALADELLFGR LTDGGRLTVD LDDKDESKTE VLLDIQPLPK KEGKSKPEEA TAG
//
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