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}.
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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
//