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Database: UniProt
Entry: A9IU97_BORPD
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Original site: A9IU97_BORPD 
ID   A9IU97_BORPD            Unreviewed;       886 AA.
AC   A9IU97;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 116.
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:CAP43516.1};
GN   OrderedLocusNames=Bpet3174 {ECO:0000313|EMBL:CAP43516.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP43516.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP43516.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; AM902716; CAP43516.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IU97; -.
DR   STRING; 94624.Bpet3174; -.
DR   KEGG; bpt:Bpet3174; -.
DR   eggNOG; COG0542; Bacteria.
DR   OMA; SKMMQGE; -.
DR   Proteomes; UP000001225; Chromosome.
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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:CAP43516.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:CAP43516.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          25..167
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          433..513
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          802..832
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   886 AA;  98482 MW;  E8F7B548D4F45EBC CRC64;
     MQVIEPAATS RRSGSPSSLT TTMRFDKLTT KFQQALADAQ SLAGRNDHPY IEPVHVLSAL
     LSDPDSGASS LLARAGVAVN RVGGPLEAAL KALPQVQGTD TVQVGRDLQA VLTRTDKEAA
     RRGDTYIASE LFLLALADDK GPAGIILRDA GLQKKALEAA IDAVRGGENV SAAEGESNRE
     ALAKYTLDLT DRARQGKLDP VIGRDDEIRR TIQILQRRTK NNPVLIGEPG VGKTAIVEGL
     AQRIVNDEVP ETLRGKRVLS LDLAALLAGA KFRGEFEERL KAVLKELAQD DGQNIVFIDE
     LHTMVGAGKA EGAMDAGNML KPALARGELH CIGATTLDEY RKYIEKDAAL ERRFQKVLVN
     EPDVESTIAI LRGLQERYEI HHGVEITDPA IVAAAELSHR YITDRFLPDK AIDLIDEAAA
     RIRMEIDSKP EVMDKLDRRI IQLKIEREAV RKESDDASKR RLAVIEEELE KLQREYNDYE
     EIWKAEKASV QGTQAIKEEI DRVRADMAEL QRKGQFDKLA ELQYGKLPEL EARLKAADTA
     EQQGEKADGQ PRLLRTQVGA EEIAEVVSRA TGIPVAKMMQ GEREKLLQME DHLHKRVVGQ
     DEAVRLVSDA IRRSRAGLAD PSRPYGSFLF LGPTGVGKTE LTRALADFLF DSEEHMIRID
     MSEFMEKHSV ARLIGAPPGY VGYEEGGYLT EAVRRKPYSV VLLDEVEKAH PDVFNVLLQV
     LDDGRLTDGQ GRTVDFRNTV IVMTSNLGSQ HIQSMAGQPY EVIKEVVWDE LKQSFRPEFL
     NRIDEVVVFH GLEAQHIESI ARIQLKRLAE RLERQEMRLE VSDAALAELA RAGFDPVFGA
     RPLKRAIQQQ IENPVAKLIL EGEFGPRDVV PVDWRDGKFV FTRTLQ
//
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