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Database: UniProt
Entry: F4AWK6_DOKS4
LinkDB: F4AWK6_DOKS4
Original site: F4AWK6_DOKS4 
ID   F4AWK6_DOKS4            Unreviewed;       868 AA.
AC   F4AWK6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Krodi_2613 {ECO:0000313|EMBL:AEE20589.1};
OS   Dokdonia sp. (strain 4H-3-7-5) (Krokinobacter sp. (strain 4H-3-7-5)).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Dokdonia.
OX   NCBI_TaxID=983548 {ECO:0000313|EMBL:AEE20589.1, ECO:0000313|Proteomes:UP000008290};
RN   [1] {ECO:0000313|EMBL:AEE20589.1, ECO:0000313|Proteomes:UP000008290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4H-3-7-5 {ECO:0000313|EMBL:AEE20589.1,
RC   ECO:0000313|Proteomes:UP000008290};
RX   PubMed=21725025; DOI=10.1128/JB.05518-11;
RA   Klippel B., Lochner A., Bruce D.C., Walston Davenport K., Detter C.,
RA   Goodwin L.A., Han J., Han S., Hauser L., Land M.L., Nolan M.,
RA   Ovchinnikova G., Pennacchio L., Pitluck S., Tapia R., Woyke T.,
RA   Wiebusch S., Basner A., Abe F., Horikoshi K., Keller M., Antranikian G.;
RT   "Complete genome sequences of Krokinobacter sp. strain 4H-3-7-5 and
RT   Lacinutrix sp. strain 5H-3-7-4, polysaccharide-degrading members of the
RT   family Flavobacteriaceae.";
RL   J. Bacteriol. 193:4545-4546(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008290}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4H-3-7-5 {ECO:0000313|Proteomes:UP000008290};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Piela B., Lochner A.,
RA   Antranikian F.I., Woyke T.;
RT   "Complete sequence of Krokinobacter diaphorus 4H-3-7-5.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4H-3-7-5;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Piela B., Lochner A.,
RA   Antranikian F.I., Woyke T.;
RT   "Complete sequence of Krokinobacter sp. 4H-3-7-5.";
RL   Submitted (FEB-2011) 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; CP002528; AEE20589.1; -; Genomic_DNA.
DR   RefSeq; WP_013752096.1; NC_015496.1.
DR   AlphaFoldDB; F4AWK6; -.
DR   STRING; 983548.Krodi_2613; -.
DR   KEGG; kdi:Krodi_2613; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_10; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000008290; 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   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;  97644 MW;  9CECE5D9479D84A7 CRC64;
     MNINNYTIKS QEAIQRAQQI AQEMGHQQIE NEHIFKAIFE IDEHVTPFLL QKLDVNIPLF
     QQVLDSTLQS YPKVSGGDIV LGREANKALT EASIIAKKMN DEYVSIEHLI LAIFSTKSKV
     AQILKDQGVT EKHLRAAIDE VRKGNRVTSQ SAEETYNSLN KYAKNLNELA RNGKLDPVIG
     RDEEIRRILQ ILTRRTKNNP ILVGEPGTGK TAIAEGLAHR IVDGDIPENL QNKQIFALDM
     GALIAGAKFK GEFEERLKAV IKEVTESDGD IVLFIDEIHT LVGAGGGQGA MDAANILKPA
     LARGELRAIG ATTLDEYQKY FEADKALERR FQKVVVDEPD TESAISILRG IKDKYETHHK
     VRIKDDAIIA AVKLSQRYIT SRFLPDKAID LMDEAAAKMR MEINSKPEEL DVLDRRVMQL
     EIEIEAIKRE KDEDKLKSLR ADLANLKEER NDLNAQWQSE KDIVESVQTA KQDIENYKIE
     AEIAEREGNY GLVAELRYGK IKDAQEHLEE LQKDLASQAD TSLIKEEVTS EDIAEVVAKW
     TGIPVQKMLQ GEREKLLQLE DELHKRVVGQ REAIVAVSDA VRRSRAGLQD QKKPIGSFLF
     LGTTGVGKTE LAKALAEYLF DDENAMTRID MSEYQERHSV SRLVGAPPGY VGYDEGGQLT
     EAVRRRPYSV VLLDEIEKAH PDTFNVLLQV LDEGRLTDNK GRTADFRNAI IIMTSNMGSH
     IIKERFEAIP DVDAAMESAK VDVLGLLKQN IRPEFLNRID DIVMFSPLTR KDIRDIVKLQ
     FKGIQKMLSQ QNITLDATKQ AIDFISEAGF QPEYGARPVK RAMQREVLNQ LSKEILSGKV
     ASDSVILVDS FDDKLVFRNE GERTGEEE
//
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