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Database: UniProt
Entry: J1F1V4_9LACO
LinkDB: J1F1V4_9LACO
Original site: J1F1V4_9LACO 
ID   J1F1V4_9LACO            Unreviewed;       865 AA.
AC   J1F1V4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=FD00_GL000956 {ECO:0000313|EMBL:KRN09546.1};
OS   Liquorilactobacillus mali KCTC 3596 = DSM 20444.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1046596 {ECO:0000313|EMBL:KRN09546.1, ECO:0000313|Proteomes:UP000050898};
RN   [1] {ECO:0000313|EMBL:KRN09546.1, ECO:0000313|Proteomes:UP000050898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20444 {ECO:0000313|EMBL:KRN09546.1,
RC   ECO:0000313|Proteomes:UP000050898};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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}.
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:KRN09546.1}.
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DR   EMBL; AYYH01000023; KRN09546.1; -; Genomic_DNA.
DR   RefSeq; WP_003690236.1; NZ_AYYH01000023.1.
DR   AlphaFoldDB; J1F1V4; -.
DR   PATRIC; fig|1046596.6.peg.1035; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000050898; 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   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          2..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..500
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   865 AA;  97387 MW;  1FA0E376EAA84E0F CRC64;
     MPEDRLTSAV QSAIAEAQQV AITRHHQEID IPEFFKVIIQ PGEFGADLFQ RTGINVGLFE
     KEIDEQLDRV SVVEGQVSYG QNFSQNLARL IQEAEQLRQK QGDEYIALDT VILALMKLKN
     HPLKIYLEKQ GLTEKKLKET IDDLRGGERV TSKNQEENYK ALEKYGIDLV KQVRSGKQDP
     VIGRDEEIRD VVRILSRKTK NNPVLIGEPG VGKTAIIEGL AQRIVRKDIP DNLKDKKIFS
     LDMGALIAGA KYRGEFEERL KSVLKEVTKS EGQIILFIDE IHNIVGAGKT EGSMDAGNLL
     KPMLARGELH LIGATTLDEY REYMEKDKAL ERRFQKVLVQ EPSVEDTISI LRGLRERFEI
     HHGVRIHDNA LVAAATLSNR YVTDRYLPDK AIDLVDEACA TIRVEMNSMP TELDQVTRQL
     MRQEVEEAAL KKESDAASKK RLAELQSELA ETREKANTLK MRWENEKEDI QKVSSKKAEL
     DKARHDLEEA ENNYDLELAA KLQHATIPQI EKELKELEQV ERPDNWLVEE SVTENEIAQV
     VSRTTGIPVA KLVQGEREKL LNLPTALHKR VIGQDEAVDA VANAVIRARA GLQDPNQPLG
     TFMFLGPTGV GKTELAKALA ENLFDSEKHM VRIDMSEYME KQSVSRLVGA APGYVGYEEG
     GQLTEAVRRN PYTIVLLDEV EKAHPDVFNI LLQVFDDGRL TDGQGRTVDF KNTIIIMTSN
     LGSGILLDNA SDGKITVETK QLVMKLAQQH FKPEFLNRID DIIMFTPLSL AAIEEIVAKF
     IDLLSSRLSE QEVELKISDE AKQWIAKEGY EPAYGARPLQ RFITNKVETP LAKEIIAGKI
     LPHSLVTITL GEEHNLIFES TEIKE
//
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