ID A0A3A9UUT8_9FLAO Unreviewed; 867 AA.
AC A0A3A9UUT8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:AXT20528.1};
GN ORFNames=D1817_11705 {ECO:0000313|EMBL:AXT20528.1};
OS Flavobacteriaceae bacterium.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1871037 {ECO:0000313|EMBL:AXT20528.1, ECO:0000313|Proteomes:UP000260281};
RN [1] {ECO:0000313|EMBL:AXT20528.1, ECO:0000313|Proteomes:UP000260281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU392 {ECO:0000313|EMBL:AXT20528.1,
RC ECO:0000313|Proteomes:UP000260281};
RA Song W., Thomas T., Edwards R.;
RT "Complete genome sequences of pooled genomic DNA from 10 marine bacteria
RT using PacBio sequencing.";
RL Submitted (AUG-2018) 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; CP031964; AXT20528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9UUT8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000260281; 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:UP000260281};
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..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 867 AA; 97908 MW; 1AC6A93055434E2F CRC64;
MNFNNYTIKS QEAIQLSQQL TQSFEHQQIE NEHLFKAIFE IDKNVLPFIL KRLNINASIL
QQVLNKELTH FPKVSEADIV LSQNTGKTIN EASIIAKKMN DEFVSIEHLI LAIFKSKSKI
AQILKDQGVT EKKLTSAITE LRKGERVTSQ SQENTYNALE KYAKNLNQLA KNGKLDPVIG
RDEEIRRILQ ILSRRTKNNP ILVGEPGTGK TAIAEGLAHR IIDGDIPENL KDKQIFALDM
GALIAGAKFK GEFEERLKSV IKEVTTSDGD VVLFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKVIVDEPD NESAISILRG IKEKYETHHK
VRIKDDAIIG AVELSSRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKVMQL
EIEIEAIKRE QDELKLKSLK SELANLKEER NTINAKWKNE KEVVDNIQNT KQIIENYKLE
AERAERDGDY GKVAELRYGK IKDAQVQLEI FQKQLQEQQN TLIKEEVTYD DIAEVVAKWT
GIPVSKMVQS EREKLLKLEN ELHKRVIGQE EAIIAVSDAV RRSRAGLQNP GKPIGSFLFL
GTTGIGKTEL AKALANYLFD DENAMTRIDM SEYQERHSIS RLVGAPPGYV GYDEGGQLTE
AVRRKPYSVV LLDEIEKAHP DTFNILLQVL DEGRLTDNKG RIADFKNTII IMTSNIGSQI
IQERFETLKD IDTATESAKL DVLGLLKQSV RPEFLNRIDD IVMFKPLSRK DIIDIVGLQL
KNVTKMIAKQ GITFDATEQA IAYLADKGYE PEYGARPVKR VIQKQVLNAL SKEMLAGKIT
TDSIILLDAF DDKLVFRNQN DLVAEEF
//