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Database: UniProt
Entry: W0SD93_9PROT
LinkDB: W0SD93_9PROT
Original site: W0SD93_9PROT 
ID   W0SD93_9PROT            Unreviewed;       758 AA.
AC   W0SD93;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:BAO28887.1};
GN   ORFNames=SUTH_01087 {ECO:0000313|EMBL:BAO28887.1};
OS   Sulfuritalea hydrogenivorans sk43H.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Sulfuritalea.
OX   NCBI_TaxID=1223802 {ECO:0000313|EMBL:BAO28887.1, ECO:0000313|Proteomes:UP000031637};
RN   [1] {ECO:0000313|EMBL:BAO28887.1, ECO:0000313|Proteomes:UP000031637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM22779 {ECO:0000313|EMBL:BAO28887.1};
RX   PubMed=25017294; DOI=10.1016/j.syapm.2014.05.010;
RA   Watanabe T., Kojima H., Fukui M.;
RT   "Complete genomes of freshwater sulfur oxidizers Sulfuricella denitrificans
RT   skB26 and Sulfuritalea hydrogenivorans sk43H: genetic insights into the
RT   sulfur oxidation pathway of betaproteobacteria.";
RL   Syst. Appl. Microbiol. 37:387-395(2014).
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; AP012547; BAO28887.1; -; Genomic_DNA.
DR   RefSeq; WP_041097663.1; NZ_AP012547.1.
DR   AlphaFoldDB; W0SD93; -.
DR   STRING; 1223802.SUTH_01087; -.
DR   KEGG; shd:SUTH_01087; -.
DR   HOGENOM; CLU_005070_4_2_4; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000031637; Chromosome.
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:BAO28887.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:BAO28887.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031637};
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"
SQ   SEQUENCE   758 AA;  82971 MW;  B92B75AAD989DCF5 CRC64;
     MIAQELEVSL HMAFVEARQK RHEFITVEHL LLALLDNPSA AEVLRACAAD IEGLRKELLT
     FINEHTPTVA GSDEIDTQPT LGFQRVIQRA ILHVQSSGKK EVTGANVLVA IFGEKDSHAV
     FFLQRQNVTR LDVVNFISHG ITKTPQPKGK DEPVETDVET QEKAGALESF TQNLNQFALA
     GKIDPLIGRD KELERVIQTL CRRRKNNPLL VGEAGVGKTA IAEGLALHIV EGRVPEILAN
     ATVYCLDMGA LLAGTKYRGD FEQRLKGVLK QLADNPNAIL FIDEIHTLIG AGAASGGTMD
     ASNLLKPALS SGTLKCIGAT TYAEFRGVFE KDHALSRRFQ KVDVNEPSVD ETVSILRGLK
     SRFEEHHGVK YSAAAISSAA ELAAKYINDR HLPDKAIDVI DEAGAAQRIL PKSKQKKTIG
     KLEIEDIVAK IARIPPQHVS ADDRSALKNL DRDLKNMVFG QEAAIDALAK AIKMSRSGLG
     DPQKPIGCFL FSGPTGVGKT EVARQLAYGM GIELIRFDMS EYMERHAVSR LIGAPPGYVG
     FDQGGLLTEA VTKKPHAVLL LDEIEKAHPE VFNILLQVMD HGTLTDNNGR KADFRNVVIV
     MTTNAGAEAL QKTSIGFTTS KGPGDEMGDI KRMFTPEFRN RLDAIISFRA LDAEIILRVV
     DKFLMQLEGQ LHEKKVEAIF TDSLRAWLAE KGFDPLMGAR PMARLIQDTI RSALADELLF
     GRLVHGGRIT IDIDEHEKIV LNFEETASTP AVPSAIQS
//
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