ID A0A085EPL0_9FLAO Unreviewed; 868 AA.
AC A0A085EPL0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=FEM08_00910 {ECO:0000313|EMBL:KFC61155.1};
OS Flavobacterium gilvum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1492737 {ECO:0000313|EMBL:KFC61155.1, ECO:0000313|Proteomes:UP000028636};
RN [1] {ECO:0000313|EMBL:KFC61155.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM1308 {ECO:0000313|EMBL:KFC61155.1};
RA Shin S.-K., Yi H.;
RT "Genome Sequence of Flavobacterium sp. EM1308.";
RL Submitted (MAY-2014) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFC61155.1}.
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DR EMBL; JNCP01000002; KFC61155.1; -; Genomic_DNA.
DR RefSeq; WP_035632961.1; NZ_JNCP01000002.1.
DR AlphaFoldDB; A0A085EPL0; -.
DR STRING; 1492737.EM308_13675; -.
DR KEGG; fgl:EM308_13675; -.
DR PATRIC; fig|1492737.3.peg.91; -.
DR eggNOG; COG0542; Bacteria.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000028636; 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: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 78, MITOCHONDRIAL; 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..487
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 97377 MW; B5915E37BAB92917 CRC64;
MNINKFTIKS QEAIQLSQQL VQSLGQQQIE NEHIFKAIFE VDENVAPFIL KKLNVNVPLF
KQILDSTIQS FPKVSGGEIQ LSRSANTTLN EAEIIAQKMN DEYVSVEHLI LAIFDSKSKV
SQILKDQGVT GKGLKAAIEE LRKGERVTSA SAEENYNSLN KYAKNLNEMA RTGKLDPVIG
RDEEIRRVLQ ILTRRTKNNP MLVGEPGVGK TAIAEGLAHR IVAGDVPENL KEKIVFSLDM
GALIAGAKYK GEFEERLKSV VKEVIAAEGD IVLFIDEIHT LVGAGGGEGA MDAANILKPA
LARGELRAIG ATTLDEYQKY FEKDKALERR FQKITIEEPD TESAISILRG IKEKYETHHK
VQIKDDAIIA AVTLSQRYIT NRFLPDKAID LMDEAASKLR MEINSKPEEL DVLDRKIMQL
EIEIEAIKRE KDEAKLKTLG LELGNLKEER NVIFAKWKSE KEVADNIQEV KTEIENFKYE
AERAERDGDY GKVAEIRYGK IKEAQDRLAD FQKQLIENKS GSSLIKEEVT REDIAEVVAK
WTGIPVMKML QGDREKLLHL EEELHHRVVG QEEAILAVSD AVRRSRAGLQ DVKKPVGTFL
FLGTTGVGKT ELAKALAEYL FDDESAMTRI DMSEYQERHS VSRLVGAPPG YVGYDEGGQL
TEAVRRKPYS VILLDEIEKA HPDTFNILLQ VLDEGRLTDN KGRLADFKNT IIIMTSNMGS
EIIQEKFENL KGSVEAATEI AKIEVLGLLK QTVRPEFINR IDEIIMFTPL TAKNIAKIVG
LQLKNVTEML AQQGITMNAT PEAVEYLSEK GFDPQFGARP VKRVIQKEVL NKLSREILAG
KIHPDSIILL DAFDNELVFR NQTELVHE
//
