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Database: UniProt
Entry: A0A0H0XQG1_9SPHN
LinkDB: A0A0H0XQG1_9SPHN
Original site: A0A0H0XQG1_9SPHN 
ID   A0A0H0XQG1_9SPHN        Unreviewed;       859 AA.
AC   A0A0H0XQG1;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AAV99_00995 {ECO:0000313|EMBL:KLI64261.1};
OS   Aurantiacibacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI64261.1, ECO:0000313|Proteomes:UP000053455};
RN   [1] {ECO:0000313|EMBL:KLI64261.1, ECO:0000313|Proteomes:UP000053455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI64261.1,
RC   ECO:0000313|Proteomes:UP000053455};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The draft genome sequence of Erythrobacter marinus HWDM-33.";
RL   Submitted (APR-2015) 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   -!- 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:KLI64261.1}.
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DR   EMBL; LBHU01000001; KLI64261.1; -; Genomic_DNA.
DR   RefSeq; WP_047092123.1; NZ_LDCP01000001.1.
DR   AlphaFoldDB; A0A0H0XQG1; -.
DR   STRING; 874156.GCA_001021555_01084; -.
DR   PATRIC; fig|874156.12.peg.209; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000053455; 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:UP000053455};
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;  94179 MW;  583183D6289DAF48 CRC64;
     MNLEKFTDRA RGFLQSAQTV AIRNSHQRIS PEHILKALLE DEEGMAAGLI QRAGGNPGTA
     VQQVDALLAK IPAVSGGGAQ QTPGLDNDAV RVLDSAEQVA AKAGDEYVTV ERLLLALALA
     KDSKAGKALA DAGLTAQALN TAINELRGGK TADSANAEAS YDAMKKYARD LTEVAREGKL
     DPVIGRDEEI RRVIQILARR TKNNPVVIGE PGTGKTAIAE GLALRIANGD VPDSLKDRRL
     MSLDLGALIA GAKYRGEFEE RLKSVLDEVK GADGEIILFI DEMHTLIGAG ASEGSMDASN
     LLKPALARGE LHCIGATTLD EYQKYVEKDA ALQRRFQPVF VDEPSVEDTI SILRGIKEKY
     ELHHGVRITD AAVVAAAQLS ERYISDRFLP DKAIDLMDEA ASRIRMEVES KPEEIENLDR
     RIFQLKIEES ALSKETDSAS EDRLKVLREE LANVEQQSSE LTTRWQNERD KINAEAKIKE
     ALDAARIELE QAQRGGDLAA AGELQYGTIP GLEKQLAEAA GHAENALLRE EVTEDDIASV
     VSRWTGIPME KMLEGEREKL LNMEDVLSKR VIGQEKAINS VSKAVRRARA GLQDPGRPMG
     SFLFLGPTGV GKTELTKALA EFLFDDDQAM VRIDMSEFME KHSVARLIGA PPGYVGYEEG
     GVLTEAVRRR PYQVVLFDEV EKAHGDVFNV LLQVLDDGHL TDGQGRKVDF SNTLIILTSN
     LGSQFLSNLG DDQTVADVED QVMEVVRSHF RPEFLNRLDE IILFHRLAME HMAPIVDIQV
     GRVQKLLKDR KIELDLTDGA RKWLGRVGYD PVYGARPLKR AVQRYLQDPL AEMLLAGEVP
     DGSTVKIDEG DGALEMVVS
//
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