GenomeNet

Database: UniProt
Entry: A0A1I6NZG4_9FLAO
LinkDB: A0A1I6NZG4_9FLAO
Original site: A0A1I6NZG4_9FLAO 
ID   A0A1I6NZG4_9FLAO        Unreviewed;       862 AA.
AC   A0A1I6NZG4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN04488006_0748 {ECO:0000313|EMBL:SFS33342.1};
OS   Lutibacter maritimus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Lutibacter.
OX   NCBI_TaxID=593133 {ECO:0000313|EMBL:SFS33342.1, ECO:0000313|Proteomes:UP000199312};
RN   [1] {ECO:0000313|Proteomes:UP000199312}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24450 {ECO:0000313|Proteomes:UP000199312};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOZP01000001; SFS33342.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6NZG4; -.
DR   STRING; 593133.SAMN04488006_0748; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199312; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:SFS33342.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFS33342.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199312};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          410..521
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   862 AA;  97191 MW;  3889D57E59A6D905 CRC64;
     MNFNKFTIKS QEAIQKAQQL AENYGHQQIE NSHILKGIFE VDENVIPFIF KKLGINIELL
     KSLIDKTLES YSKVTGGEIS LSRNASKMLN NATDEASKMN DEFVSIEHLL LALLNTKDTT
     SQILKDQGVT EKGLKIAIDE LRKGSKVTSQ SAEETYNSLN KYAKNLNQLA KDGKLDPVIG
     RDEEIRRILQ ILSRRTKNNP MLVGEPGTGK TAIAEGLAHR IVKGDIPENL KDKQIYSLDM
     GALIAGAKYK GEFEERLKSV IKEVTSAEGE IVLFIDEIHT LVGAGGGQGA MDAANILKPA
     LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVMVNEPD TESAISILRG IKEKYENHHK
     VQIKDDAIIA AVELSQRYIS NRFLPDKAID LMDEAAAKLR MEINSKPEEL DVLDRKIMQI
     EIEIEAIKRE NDEKKLASLK EELANLKEKR NEINAKWVSE KELVDSIQAS KEAIENFKLD
     AERAEREGDY GKVAEIRYGK IKEEQEKLDK LQVELNENQS SALIKEEVTR DDIAEVVAKW
     TGIPVSKMLQ SEREKLLLLE DELHNRVVGQ EEGIAAVADA VRRSRAGLQD SKRPIGTFLF
     LGTTGVGKTE LAKALAEYLF DDENSLTRID MSEYQERHSV SRLVGAPPGY VGYDEGGQLT
     EAVRRKPYSV ILLDEIEKAH PDTFNILLQV LDEGRLTDNK GRLADFRNTI IIMTSNMGSQ
     IIQERFEKMD MKNRDAITDV TKLEVVALLK QTIRPEFLNR IDEIVMFTPL NESEIKQIVK
     LQLNGLIKML KAQDIQIEYT EDLVDSLAIK GFDPQFGARP VKRVIQKEVL NELSKEILSG
     KVTATSRILL DAFDDKIVFR NK
//
DBGET integrated database retrieval system