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Database: UniProt
Entry: A0A2U1C4S9_9BURK
LinkDB: A0A2U1C4S9_9BURK
Original site: A0A2U1C4S9_9BURK 
ID   A0A2U1C4S9_9BURK        Unreviewed;       783 AA.
AC   A0A2U1C4S9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:PVY55930.1};
GN   ORFNames=C8D04_1147 {ECO:0000313|EMBL:PVY55930.1};
OS   Simplicispira sp. 125.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Simplicispira.
OX   NCBI_TaxID=2135643 {ECO:0000313|EMBL:PVY55930.1, ECO:0000313|Proteomes:UP000245599};
RN   [1] {ECO:0000313|EMBL:PVY55930.1, ECO:0000313|Proteomes:UP000245599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=125 {ECO:0000313|EMBL:PVY55930.1,
RC   ECO:0000313|Proteomes:UP000245599};
RA   Chistoserdova L.;
RT   "Synthetic bacterial communities of pure cultures isolated from sediment of
RT   Lake Washington, USA.";
RL   Submitted (APR-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:PVY55930.1}.
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DR   EMBL; QEKM01000001; PVY55930.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U1C4S9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000245599; 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:PVY55930.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:PVY55930.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245599};
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          144..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   783 AA;  85782 MW;  5855EA19B96BA587 CRC64;
     MIAQELEVSL HMAFVEARQQ RHEFITVEHL LLALLDNPSA AEVLRACSAN IDDLRSSLAN
     FIKDNTPQVA GTDEVDTQPT LGFQRVIQRA IMHVQSTGNG KKEVNGANVL VAIFGEKDSH
     AVYYLHQQGV TRLDVVNFIA HGIKKGEPPE PAKGSEGPAE NEEGPSGEKS EKASPLEQFT
     QNLNQLAKDG KIDPLIGRHF EVERTIQILC RRRKNNPLLV GEAGVGKTAI AEGLAWRITQ
     NDVPEILAEA VVYSLDMGAL LAGTKYRGDF EQRLKGVLKS LKDKPNAILF IDEIHTLIGA
     GAASGGTLDA SNLLKPALSS GALKCIGATT FTEYRGIFEK DAALSRRFQK VDVVEPTVQE
     TIDILKGLKS RFEEHHSVKY AAAALQAAAE LSAKYINDRH LPDKAIDVID EAGAAQRILV
     PSKRKKTIGK TEIEEIVAKI ARIPPANVSN DDRGKLQTLE RDLKSVVFGQ DKALEVLASS
     VKMARSGLGK GDKPIGSFLF SGPTGVGKTE AAKQLAYILG IELIRFDMSE YMERHAVSRM
     IGAPPGYVGF DQGGLLTEAV TKKPHSVLLL DEIEKAHPDI FNVLLQVMDH GTLTDNNGRK
     ADFRNVIIIM TTNAGAETMN KATIGFTNPR QAGDEMGDIK RLFTPEFRNR LDAIVSFKAL
     DEQIILRVVD KFLLQLETQL AEKKVEVTFT DTLRKFLAKK GFDPLMGARP MQRLIQDTIR
     RALADELLFG RLQDGGRLTV DMDVKTDEKG VETGEVLLDI QPLPKKERLA KSEPAEPEEA
     TAG
//
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