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Database: UniProt
Entry: A0A0F6AFR9_9GAMM
LinkDB: A0A0F6AFR9_9GAMM
Original site: A0A0F6AFR9_9GAMM 
ID   A0A0F6AFR9_9GAMM        Unreviewed;       858 AA.
AC   A0A0F6AFR9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=N479_06370 {ECO:0000313|EMBL:KKE85055.1};
OS   Pseudoalteromonas luteoviolacea S4054.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1129367 {ECO:0000313|EMBL:KKE85055.1, ECO:0000313|Proteomes:UP000033434};
RN   [1] {ECO:0000313|EMBL:KKE85055.1, ECO:0000313|Proteomes:UP000033434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4054 {ECO:0000313|EMBL:KKE85055.1,
RC   ECO:0000313|Proteomes:UP000033434};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(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. {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:KKE85055.1}.
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DR   EMBL; AUXW01000079; KKE85055.1; -; Genomic_DNA.
DR   RefSeq; WP_046354723.1; NZ_AUXW01000079.1.
DR   AlphaFoldDB; A0A0F6AFR9; -.
DR   PATRIC; fig|1129367.4.peg.908; -.
DR   Proteomes; UP000033434; 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          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          405..461
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   858 AA;  95972 MW;  4D76F0C1B3DA9640 CRC64;
     MRLDRFTSKF QSALSDAQSL ALGRDHQFIE PVHLMYALLQ QTGSSVRALF AQAGVSADEL
     NTKLSQSIER LFKVEGVGGD VQLSNNLISL INLCDKYAQK RKDKYISSEV FVFSACEDKG
     ELGDIFRALN ITQDKVEKAI KAIRGGQKVD DPNAEETRQA LEKYTIDLTE RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKHKRVLSL
     DLGALVAGAK YRGEFEERLK SVLNELAKEE GSVILFIDEI HTMVGAGKTD GAMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVSE PTVEDTIAIL RGLKERYELH
     HSVDITDPAI VAAANLSHRY ISDRQLPDKA IDLIDEAGSS IRLQIDSKPE QLDKLERRII
     QLKLEDNALA KEKDEASQKR RTEMQSLISQ LETEYTELDE VWNAEKASLQ GTQVIKAELE
     QARLDLEVAR RASDLQRMSE LQYGRIPALE RKLDLASQAE MQEMSLLKNQ VSEDEIAEIL
     SRWTGIPVAK MLQGEREKLL HMEDELHQKV IGQDEAVNAI ANAIRRSRAG LADPNRPIGS
     FLFLGPTGVG KTELTKALAN FMFDTEDAMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
     YLTEAVRRRP YSVVLLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFK NTVIIMTSNL
     GSDVIQEQAS SNDYAGLKNK LMDVLTTQFR PEFINRIDET VVFHPLVTEH IKQIARIQLD
     KLSSRLKDNG YMFEVSESAL EKIAQSGFDP VFGARPLKRA IQQYIENPLA QSLLQGDFSG
     FNAIKVDVNE DTIQFTGQ
//
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