ID A0A1H1WBK6_9FLAO Unreviewed; 868 AA.
AC A0A1H1WBK6;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN04489797_2824 {ECO:0000313|EMBL:SDS94493.1};
OS Winogradskyella sediminis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Winogradskyella.
OX NCBI_TaxID=1382466 {ECO:0000313|EMBL:SDS94493.1, ECO:0000313|Proteomes:UP000198963};
RN [1] {ECO:0000313|EMBL:SDS94493.1, ECO:0000313|Proteomes:UP000198963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA_55 {ECO:0000313|EMBL:SDS94493.1,
RC ECO:0000313|Proteomes:UP000198963};
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; LT629774; SDS94493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1WBK6; -.
DR STRING; 1249933.SAMN04489797_2824; -.
DR Proteomes; UP000198963; Chromosome I.
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:SDS94493.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SDS94493.1};
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 868 AA; 97640 MW; 54828733234482A4 CRC64;
MNFNNYTIKS QEAIQQAQQL AQGFGHQQIE NEHIFKSLFT VDENVLPFLL KKLNVNVTIL
QQIVDKELES FPKVSGGDIM LSREASKTLN EASIIAKKMN DDFVSIEHLI LAIFKSKSKI
AQILKDQGVT EKGLNTAIDE LRKGDRVTSQ SQEETYNSLS KYAKNLNQLA QDGKLDPVIG
RDEEIRRILQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IIDGDIPENL KDKQIFALDM
GALIAGAKYK GEFEERLKAV IKEVTESNGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQMVNVDEPD TESAISILRG IKEKYEAHHK
VQIKDEAIIG AVELSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
EIEHEAIKRE KDETKLKSLK AELANLKEER NELNAKWKSE KEVVDNVQNI KEQIENFKLE
AERAERDGDY GKVAEIRYGK IKEANAQLEK FQKELSEQNE TSLIKEEVTY EDIAEVVAKW
TGIPVTKMLQ SDREKLLKLE DELHKRVVGQ EEAIEAVSDA VRRSRAGLQN PQKPVGTFLF
LGTTGVGKTE LAKALAEYLF DDENAMTRID MSEYQERHAV SRLVGAPPGY VGYDEGGQLT
EAVRRKPYSV VLLDEIEKAH PDTFNILLQV LDEGRLTDNK GRVADFKNTI IIMTSNMGSQ
IIQERFEATK DIPSAIEAAK VDVLAILKQS VRPEFLNRID DTIMFTPLSK ENIIDIVGLQ
LKGITKMIAK QGITFDATPE AVSYLADKGY NPEYGARPVK RVIQKDVLNQ LSKEILAGRV
TTDSIILLDE FDNHLVFRNQ GDLVVEKM
//