ID A0A553EXU8_9BACT Unreviewed; 869 AA.
AC A0A553EXU8;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TRX49830.1};
GN ORFNames=FNH22_26360 {ECO:0000313|EMBL:TRX49830.1};
OS Fulvivirga sp. M361.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Fulvivirgaceae;
OC Fulvivirga.
OX NCBI_TaxID=2594266 {ECO:0000313|EMBL:TRX49830.1, ECO:0000313|Proteomes:UP000317847};
RN [1] {ECO:0000313|EMBL:TRX49830.1, ECO:0000313|Proteomes:UP000317847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M361 {ECO:0000313|EMBL:TRX49830.1,
RC ECO:0000313|Proteomes:UP000317847};
RA Meng X.;
RT "Draft genome seqence of M361 submission.";
RL Submitted (JUL-2019) 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:TRX49830.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VKDC01000038; TRX49830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A553EXU8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000317847; 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 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:UP000317847};
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 396..528
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 869 AA; 97413 MW; 67E725ED349BAEE0 CRC64;
MNFDKYTIKS QEALQKAAEV ASGNGQQAIE TGHLLVAVLK TDENVISFLV KKLDINSGLL
DTKLEEIIQG YPKVSGQQPY LSNAAAGALQ KAEKQLKEFG DEYIAIEHIL LGLLEGGDKV
AGIMKDVGFN KKSLIAGIKE LRGGDTVKDQ NAESKYRSLE RYSINLNEQA KSGKIDPVIG
RDDEIRRVLQ ILSRRTKNNP ILLGEPGVGK TAIVEGMAQR IVDGDVPENL KDKILISLDM
GLLVAGAKYK GEFEERLKSV IKEVTDSEGQ IILFIDEIHT LIGAGGGEGA MDAANLLKPA
LARGELHAIG ATTLKEYQKY VEKDKALERR FQSVTVDEPS GPDAISILRG IKDKYELHHG
VRIKDDAVIA AVELSSRYIS DRYLPDKAID LMDEAAAKLR LEMDSLPEEL DELNRKIMQL
EIEREAIRRE KNKDKERILT KDIAELASER NDLKARWENE KTIVQGIRDE KENIDKLKFE
AEQAEKAGDF GSVAEIRYGK LVEAEKKLEE LQNHVKETQG EDSLLKEEVD NEDIAEVVAK
WTGIPVSKML QSDREKLLHL EVELGKRIAG QEEAIMALSD AVRRSRAGLQ DPRRPIGSFI
FLGTTGVGKT ELSKALAEYL FNDENAMVRI DMSEYQERHA VSRLVGAPPG YVGYDEGGQL
TEAVRRKPYS VILLDEIEKA HPDVFNVLLQ VLDDGRLTDN KGRVANFKNT IIIMTTNIGS
HVIQEKFERL TEDNVEEILS ATKQDVYELL KRSVRPEFLN RVDETIMFRP LSRTDIRKVV
DIQFRLIKQR LMEAGVKIEI SDKALDHLAE IGFDPQFGAR PLKRVIQREI LNEFSKEILA
GRVNKESLVG VDVRDNGEIE FINLDEVEI
//