ID A0A1G8NG67_9RHOO Unreviewed; 754 AA.
AC A0A1G8NG67;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SDI79158.1};
GN ORFNames=SAMN05660652_04044 {ECO:0000313|EMBL:SDI79158.1};
OS Propionivibrio dicarboxylicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=83767 {ECO:0000313|EMBL:SDI79158.1, ECO:0000313|Proteomes:UP000198607};
RN [1] {ECO:0000313|EMBL:SDI79158.1, ECO:0000313|Proteomes:UP000198607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5885 {ECO:0000313|EMBL:SDI79158.1,
RC ECO:0000313|Proteomes:UP000198607};
RA de Groot N.N.;
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}.
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DR EMBL; FNCY01000030; SDI79158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8NG67; -.
DR STRING; 83767.SAMN05660652_04044; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000198607; 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:SDI79158.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDI79158.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198607};
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 144..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 82623 MW; A0D7D94DBCCB93C8 CRC64;
MIAQELEVSL HMAFVEARQK RHEFITVEHL LLALLDNPSA AEALRACGGN IEQLRRDLNK
FIGEHTPRIE GEDEIDTQPT LGFQRVIQRA ILHVQSSGKK EVNGANVLVA IFGEKDSHAV
YYLQKQGITR LDVVNFISHG VSKVQPNAPR AEPEGETEAE GQQNAAGPLE SYTINLNALA
LQGKIDPLIG RDQELERVIQ TLCRRRKNNP LLVGEAGVGK TAIAEGLARK IVENDVPEIL
AQANVYALDM GALLAGTKYR GDFEQRLKAV LKQLGENPNA ILFIDEIHTL IGAGSASGGT
MDASNLLKPA LSSGLIKCIG ATTYNEYRGI FEKDHALSRR FQKIDVNEPS SADTIDILKG
LKSRFESHHG IKYSAAALTS AVDLSVRFIT DRHLPDKAID VIDEAGAAQR ILPKSKQKKL
IGKQDIEEIV AKIARVPSTQ VSSDDRSALK NLDRDLKAVV FGQDVAIDAL AKAIKMARSG
LGTPGKPIGS FLFSGPTGVG KTEVAKQLAY CLGVELLRFD MSEYMERHAV SRLIGAPPGY
VGFDQGGQLT EAVTKKPYCV LLLDEIEKAH PDIYSILLQV MDHGTLTDNN GRKADFRNVI
IIMTTNAGQE SLQKATMGFT SARAVGDEMV DIKRIFSPEF RNRLDAIISF KPLDHDIILR
VVDKFLMQLE EQLHEKKVEV AFTDTLKDHL ATKGFDPLMG ARPMSRLIQD VIRAALADEL
LFGRLVNGGH VTVDIGPDDK IRLSYASEKD PVVA
//