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Database: UniProt
Entry: A0A0D8PL17_9GAMM
LinkDB: A0A0D8PL17_9GAMM
Original site: A0A0D8PL17_9GAMM 
ID   A0A0D8PL17_9GAMM        Unreviewed;       859 AA.
AC   A0A0D8PL17;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=C9I88_19485 {ECO:0000313|EMBL:PSV88872.1};
OS   Photobacterium iliopiscarium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=56192 {ECO:0000313|EMBL:PSV88872.1, ECO:0000313|Proteomes:UP000241954};
RN   [1] {ECO:0000313|EMBL:PSV88872.1, ECO:0000313|Proteomes:UP000241954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCIMB 13481 {ECO:0000313|EMBL:PSV88872.1,
RC   ECO:0000313|Proteomes:UP000241954};
RA   Butler K.;
RT   "Whole genome sequencing of Histamine producing bacteria.";
RL   Submitted (JAN-2018) 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. {ECO:0000256|RuleBase:RU362034}.
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:PSV88872.1}.
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DR   EMBL; PYLW01000037; PSV88872.1; -; Genomic_DNA.
DR   RefSeq; WP_045038604.1; NZ_PYOP01000043.1.
DR   AlphaFoldDB; A0A0D8PL17; -.
DR   STRING; 56192.UB38_10475; -.
DR   GeneID; 70040847; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000241954; 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 78, MITOCHONDRIAL; 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          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..462
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   859 AA;  96038 MW;  E219AFADC999D53C CRC64;
     MRLDRFTSKF QAAISDAQSL ALGRDHQYIE PAHLMVALLN QEGSTVRPLL TLLNVDSTQL
     RSRLGEILER IPKVTGIGGE VQLSNSMGTL LNMCDKLAQK RNDKFISSEL FILAVVDNDK
     GPLGDLLREL GLKADQIGKA IDQIRGGQKV DDQNAEENRQ ALSKYTIDLT ERAEQGRLDP
     VIGRDDEIRR TIQVLQRRTK NNPVIIGEPG VGKTAIVEGL AQRIVNGEVP EGLRDKRVLS
     LDMGSLIAGA KFRGEFEERL KAVLNELSQE DGRIILFIDE IHTMVGAGKG EGSMDAGNML
     KPALARGDLH CVGATTLNEY RQYLEKDAAL ERRFQKVLVD EPSVEDTIAI LRGLKERYEL
     HHHVEITDPA IVAAATLSHR YISDRQLPDK AIDLIDEAAS SIRMQIDSKP ESMDRLERRI
     IQLKIEQQAL EKESDDASQK RLSNLLEELD IKEREYSELE EVWNAEKASL SGTQHIKTEL
     EQARTDVEIA RRAGDLNRMS ELQYGRIPEL EKQLDLAAQA EMQDMTLLKN KVTDVEIADV
     LSKATGIPVA KMLEGERDKL LRMEDELHNR VIGQEEAVEA VANAIRRSRA GLSDPQRPIG
     SFLFLGPTGV GKTELCKSLA NFMFDSEDAM VRIDMSEFME KHSVARLVGA PPGYVGYEEG
     GYLTEAVRRR PYSVILLDEV EKAHPDVFNI LLQVLDDGRL TDGQGRTVDF RNTVIIMTSN
     LGSDRIQEHF GSLDYEGIKA LVMEVVGQHF RPEFINRVDE TVVFHPLGKD NIKHIASIQL
     ARLEKRLAEK DFQLEVEESA LELISDAGFD PVFGARPLKR AIQQYIENPL AQDLLSGKFM
     PGKPIVLSVE DDKIVAKQA
//
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