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Database: UniProt
Entry: K7AA67_9ALTE
LinkDB: K7AA67_9ALTE
Original site: K7AA67_9ALTE 
ID   K7AA67_9ALTE            Unreviewed;       856 AA.
AC   K7AA67;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=C427_3838 {ECO:0000313|EMBL:AGH45943.1};
OS   Paraglaciecola psychrophila 170.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH45943.1, ECO:0000313|Proteomes:UP000011864};
RN   [1] {ECO:0000313|EMBL:AGH45943.1, ECO:0000313|Proteomes:UP000011864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:AGH45943.1,
RC   ECO:0000313|Proteomes:UP000011864};
RX   PubMed=23640379;
RA   Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT   "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL   Genome Announc. 1:E00199-13(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}.
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DR   EMBL; CP003837; AGH45943.1; -; Genomic_DNA.
DR   RefSeq; WP_007641061.1; NZ_BAES01000068.1.
DR   AlphaFoldDB; K7AA67; -.
DR   STRING; 1129794.C427_3838; -.
DR   KEGG; gps:C427_3838; -.
DR   PATRIC; fig|1129794.4.peg.3823; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_6; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000011864; 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   Reference proteome {ECO:0000313|Proteomes:UP000011864};
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..449
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   856 AA;  94908 MW;  2FB1F35E11A1D442 CRC64;
     MRLDSFTSKF QTAISEAQSL ALGRDHQYIE PVHLMTALLN QQGGSVRPLF DQANINVNSL
     RSALAEALGR LPRIEGTGGD VQLGKSTVVL LNLSDKIAQK RKDDYITSEV FVLAALQDKG
     SLGALLKQSG ADQEKIEKAI EKMRGGQKVT DQNAEDVRQA LDKFTTDLTA RAEQGKLDPV
     IGRDDEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIAEGLA QRIINSEVPE GLKNKRVLSL
     DMGSLIAGAK FRGEFEERLK AVLNELSKEE GRVILFIDEL HTMVGAGKGE GAMDAGNMLK
     PALARGELHC VGATTLNEYR QYIEKDAALE RRFQKVLVEE PSVEDTIAIL RGLKERYELH
     HSVEITDPAI VAAASLSHRY ISDRQLPDKA IDLIDEAASS IRLQMDSKPE DMDKLERRII
     QLKLEEQALS KEKDEASHKR LELIELEREQ AEHKFSAFET IWIAEKQAMQ GTQTIRSELE
     QAKLDLEIAR RASDLSRMSE LQYGRIPELE AKLEVATESE TQETTLLKNK VTESEIADVL
     SRWTGIPVSK MLEGEKVKLL AMEEALHKRV VGQSEAVTAV ANAIRRSRAG LSDPNRPIGS
     FLFLGPTGVG KTELCKTLAN FLFDTENAMV RIDMSEFMEK HSVARMVGAP PGYVGYEEGG
     YLTEAVRRKP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFK NTVIIMTSNL
     GSDIIQEVSG ESNYQQMKGL VMNAVGEHFR PEFLNRVDDI VVFHPLGKEQ IKAIAKIQLC
     SLRERLAEKG YKLELSLEAL DKIADAGFDP VYGARPLKRA IQTEIENPLA QKILAGTLGV
     DGVVTIDVKA DKMTII
//
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