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Database: UniProt
Entry: A0A1G8NG67_9RHOO
LinkDB: A0A1G8NG67_9RHOO
Original site: A0A1G8NG67_9RHOO 
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
//
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