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Database: UniProt
Entry: R9PJJ4_AGAAL
LinkDB: R9PJJ4_AGAAL
Original site: R9PJJ4_AGAAL 
ID   R9PJJ4_AGAAL            Unreviewed;       856 AA.
AC   R9PJJ4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AALB_1607 {ECO:0000313|EMBL:GAD01527.1};
OS   Agarivorans albus MKT 106.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Agarivorans.
OX   NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD01527.1, ECO:0000313|Proteomes:UP000014461};
RN   [1] {ECO:0000313|EMBL:GAD01527.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., Sano M.;
RT   "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an Agarolytic
RT   Marine Bacterium.";
RL   Genome Announc. 1:e00367-13(2013).
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:GAD01527.1}.
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DR   EMBL; BARX01000009; GAD01527.1; -; Genomic_DNA.
DR   RefSeq; WP_016401295.1; NZ_BARX01000009.1.
DR   AlphaFoldDB; R9PJJ4; -.
DR   STRING; 1331007.AALB_1607; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000014461; 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   Reference proteome {ECO:0000313|Proteomes:UP000014461};
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   856 AA;  95671 MW;  EE218C11A20FE614 CRC64;
     MRLDRFTSKF QLAISDAQSL ALGRDHQFIE PVHLMSAMLN QDAASLRPLL VEAGIEGSAL
     RSQLSQALEQ LPRVEGTGGE VQLSNQLVVL LNLCDKLAQK RKDKFISSEI FFLAVTEDKG
     KLGDIMRELG ANKENIEKAI TKIRGGQKVD DPNAEDQRQA LEKYTIDLTE RAEQGKLDPV
     IGRDDEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIINHEVPE GLKNKRVLSL
     DMGSLVAGAK YRGEFEERLK AVLNELSQEE GQVILFIDEL HTMVGAGKGD GAMDAGNMLK
     PALARGELHC VGATTLNEYR QYIEKDAALE RRFQKVLVEE PNVEDTIAIL RGLKERYELH
     HSVEITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRLQIDSKPE ALDKLERKII
     QLKLERQALQ KEADSASLKR LALLDEELAE KESKFKELDE VWKAEKAALS GTQHIKADLE
     QARLDMDVAR RAGDLNRMSE LQYGRIPELE RQLDLASQAE MQDMSLLRNK VSDAEIADVL
     SRWTGIPVNR MLEGERDKLL RMEQQLHDRV IGQGEAVEAV SNAIRRSRAG LSDPNRPIGS
     FLFLGPTGVG KTELCKALAE FMFDTEESMV RIDMSEFMEK HSVARLVGAP PGYVGYEEGG
     YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NAVIIMTSNL
     GSDIIQERHG EMTHQEIKTA LMGVLAQQFR PEFINRIDES VVFHPLAHEQ IRTIAGIQVQ
     RLVPRLEEKG YKLEFSDAVL DKLGQAGFDP VYGARPLKRA IQQQLENPLA QAILSGQIEP
     GKTIRIELED GQLAFK
//
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