GenomeNet

Database: UniProt
Entry: A0A173KXF8_9SPHN
LinkDB: A0A173KXF8_9SPHN
Original site: A0A173KXF8_9SPHN 
ID   A0A173KXF8_9SPHN        Unreviewed;       859 AA.
AC   A0A173KXF8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=EP837_01549 {ECO:0000313|EMBL:ANI77965.1};
OS   Sphingobium sp. EP60837.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1855519 {ECO:0000313|EMBL:ANI77965.1, ECO:0000313|Proteomes:UP000078304};
RN   [1] {ECO:0000313|EMBL:ANI77965.1, ECO:0000313|Proteomes:UP000078304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EP60837 {ECO:0000313|EMBL:ANI77965.1,
RC   ECO:0000313|Proteomes:UP000078304};
RA   Lee C.-M., Yoon S.-H., Kim B.-Y.;
RT   "Complete genome sequence of a organophosphorus pesticides.";
RL   Submitted (JUN-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   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP015986; ANI77965.1; -; Genomic_DNA.
DR   RefSeq; WP_066526088.1; NZ_CP015986.1.
DR   AlphaFoldDB; A0A173KXF8; -.
DR   STRING; 1855519.EP837_01549; -.
DR   KEGG; sphb:EP837_01549; -.
DR   PATRIC; fig|1855519.3.peg.1581; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000078304; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
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; TIGR03346; chaperone_ClpB; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078304};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          415..495
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   859 AA;  93592 MW;  752788ECDD8053BA CRC64;
     MNLEKFTDRA KGFLQSAQTV AIRMSHQRIS PEHLLKALLE DSQGMASGLI KAAGGDPAVA
     VRETDSALAK VPAVSGSGAQ QTPGLDNDAV RVLDSAEQVA AKAGDSFVTV ERLLLALTLA
     TTTAAGKALA AAGVKAEGLN AAINNLRGGR TADTVGAEDR YDALKKFARD LTEAAREGKL
     DPVIGRDEEI RRTIQILARR TKNNPVLIGD PGVGKTAIAE GLALRIANGD VPDTLKDRTL
     MALDMGSLIA GAKYRGEFEE RLKGVLDEVK GAEGQIVLFI DEMHTLIGAG KSEGAMDAGN
     LLKPALARGE LHCIGATTLD EYRKYVEKDP ALQRRFQPVF VGEPTVEDTI SILRGLKEKY
     ELHHGVRITD GAIVSAATLS NRYITDRFLP DKAIDLMDEA ASRLRMEVES KPEEIENLDR
     RIIQLKIERE ALKKETDKAS KDRLAALEED LANLEQQSAA LTQRWQAEKD KIAGESKLKE
     QLDAARVELE QAQRAGDLAK AGELAYGRIP ELERKIAEVE GATEDAMLRE EVTSEDIASV
     VSRWTGIPVD KMMEGEREKL LAMEEELGKR VIGQADAVKA VATAVRRSRA GLQDPNRPLG
     SFLFLGPTGV GKTELTKALA GFLFDDDSAM VRIDMSEFME KHSVARLIGA PPGYVGYEEG
     GVLTEAVRRR PYQVVLFDEV EKAHGDVFNV LLQVLDDGRL TDGQGRTVDF TNTIIVLTSN
     LGSQFIASLA DDEPVEKVED QVMDIVRAHF RPEFLNRLDE VILFHRLGAS HMAPIVDIQV
     GRVQKLLKDR KVVLDLTDGA RAWLGRVGYD PVYGARPLKR AVQRYLQDPL ADLILRGEVP
     DGSRVKVDEG DGALQLTVG
//
DBGET integrated database retrieval system