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Database: UniProt
Entry: A0A411PJK7_9GAMM
LinkDB: A0A411PJK7_9GAMM
Original site: A0A411PJK7_9GAMM 
ID   A0A411PJK7_9GAMM        Unreviewed;       857 AA.
AC   A0A411PJK7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
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:QBF83684.1};
GN   ORFNames=EXU30_14010 {ECO:0000313|EMBL:QBF83684.1};
OS   Shewanella maritima.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=2520507 {ECO:0000313|EMBL:QBF83684.1, ECO:0000313|Proteomes:UP000291106};
RN   [1] {ECO:0000313|EMBL:QBF83684.1, ECO:0000313|Proteomes:UP000291106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D4-2 {ECO:0000313|EMBL:QBF83684.1,
RC   ECO:0000313|Proteomes:UP000291106};
RA   Baek K.;
RT   "Shewanella sp. D4-2 isolated from Dokdo Island.";
RL   Submitted (FEB-2019) 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}.
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DR   EMBL; CP036200; QBF83684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411PJK7; -.
DR   KEGG; smai:EXU30_14010; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000291106; 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: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          412..461
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   857 AA;  95544 MW;  69E46F7136DA9E82 CRC64;
     MRLDRMTNKF QIAISDAQSL ALGRDHQFIE PTHLMMALLN QDSGSIHPLL TQAGIQVSAL
     RSKLSQELER LPQVEGTGAD VQLSQGLIRL LNLCDKLSQK RKDKYISSEL FIIAALEGND
     ALSKALKESG ATKELMEKSI EQMRGGQNVD DPNAEDQRQA LKKFTIDLTE RAEQGKLDPV
     IGRDDEIRRT IQVLQRRSKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GIKNKRVLSL
     DMGALIAGAK YRGEFEERLK AVLNELAQEE GQIILFIDEL HTMVGAGKGE GAMDAGNMLK
     PALARGELHC VGATTLDEYR QYVEKDAALE RRFQKVVVDE PSVEATIAIL RGLKERYELH
     HHVEITDPAI VAAASMSHRY ISDRKLPDKA IDLIDEAASS IRLQIDSKPE TLDRLERRAI
     QLKLEEQALA KESDEASRKR LSHLQSELKE VELNANELNE IWHTEKAALA GTQHIKADLE
     QARMDLEVAR RASDLTRMSE LQYGRIPELE KQLDLASQAE MQDMTLLRNK VTDVEIAEVL
     SKATGIPVAK MLEGEREKLL HMEDALHERV IGQNEAVDAV ANAIRRSRAG LADPNRPIGS
     FLFLGPTGVG KTELCKSLAK FLFDTESAMV RIDMSEFMEK HAVSRLVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
     GSDVIQEQFE QLDYQSMKQQ VMNVVTHSFR PEFLNRVDES VVFHPLAAEH IAHIASIQLN
     NLKQRLAERD FDIEISKDAL ALIAQAGFDP VYGARPLKRA LQQEVENPLA QLLLKGELVP
     GKVIKVDVVD SQLMFNQ
//
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