GenomeNet

Database: UniProt
Entry: A0A502CLU2_9SPHN
LinkDB: A0A502CLU2_9SPHN
Original site: A0A502CLU2_9SPHN 
ID   A0A502CLU2_9SPHN        Unreviewed;       859 AA.
AC   A0A502CLU2;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:TPG13594.1};
GN   ORFNames=EAH84_05250 {ECO:0000313|EMBL:TPG13594.1};
OS   Sphingomonas oligophenolica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=301154 {ECO:0000313|EMBL:TPG13594.1, ECO:0000313|Proteomes:UP000318413};
RN   [1] {ECO:0000313|EMBL:TPG13594.1, ECO:0000313|Proteomes:UP000318413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5.1 {ECO:0000313|EMBL:TPG13594.1,
RC   ECO:0000313|Proteomes:UP000318413};
RX   PubMed=31206918;
RA   Altshuler I., Hamel J., Turney S., Magnuson E., Levesque R., Greer C.,
RA   Whyte L.G.;
RT   "Species interactions and distinct microbial communities in high Arctic
RT   permafrost affected cryosols are associated with the CH4 and CO2 gas
RT   fluxes.";
RL   Environ. Microbiol. 0:0-0(2019).
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   -!- 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:TPG13594.1}.
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; RCZK01000003; TPG13594.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A502CLU2; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000318413; Unassembled WGS sequence.
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:UP000318413};
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;  93677 MW;  A1348663407C0EFC CRC64;
     MNLEKFTDRA KGFLQSAQTV AIRMNHQRIA PEHLLKALLE DDQGMAAGLV TAAGGDARKA
     TSETDLALSK IPAVSGSGAQ QTPGLDNDAV RVLDSAEQIA AKAGDSYVTV ERLLVALALG
     LNAAAGKALK AAGATPEKLN AAINDLRGGR TADTASAEDR YDALKKFARD LTQAARDGKL
     DPVIGRDEEI RRTIQILARR TKNNPALIGE PGVGKTAIAE GLALRIANGD VPDTLKGRTL
     MSLDMGALIA GAKYRGEFEE RLKGVLDEVK AADGDIVLFI DEMHQLIGAG KSEGAMDAGN
     LLKPALARGE LHCVGATTLD EYRKYVEKDP ALQRRFQPVF VGEPTVEDTI SILRGLKDRY
     ELHHGVRITD ASLVAAATLS NRYITDRFLP DKAIDLMDEA ASRIRMEVES KPEEIETLDR
     RIIQLKIERE ALRRETDAAS VDRLATLEGD LANLEQQSSE LTTRWQAEKD KIGAEAKLKE
     QLDAARIELD QAQREGNLAR AGELSYGTIP QLSKQLDDAQ GQTKGAMLRE EVTADDIAGV
     VSRWTGIPVD RMLQGERDKL LRMEEVIGKR VIGQAEAVRA VSTAVRRARA GLQDANRPLG
     SFLFLGPTGV GKTELTKALA EFLFDDGNAM VRIDMSEFME KHAVARLIGA PPGYVGYEEG
     GVLTEAVRRR PYQVVLFDEV EKAHGDVFNI LLQVLDDGRL TDGQGRTVDF SNTLIILTSN
     LGSQYLANLD EGQDVESVEP QVMEIVRGHF RPEFLNRLDD IILFHRLGQA HMAPIVDIQV
     ARVDKLLADR KITLALTDAA RAWLGRVGYD PVYGARPLRR AVQRYLQDPL ADLILRGDVK
     DGSTVDVDES DGKLTLTVV
//
DBGET integrated database retrieval system