ID A0A1W6ECQ2_9BACT Unreviewed; 883 AA.
AC A0A1W6ECQ2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=A6C57_24060 {ECO:0000313|EMBL:ARK13162.1};
OS Fibrella sp. ES10-3-2-2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1834519 {ECO:0000313|EMBL:ARK13162.1, ECO:0000313|Proteomes:UP000193660};
RN [1] {ECO:0000313|Proteomes:UP000193660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES10-3-2-2 {ECO:0000313|Proteomes:UP000193660};
RA Kim M.K., Srinivasan S., Kim E.B., Kim K.S.;
RL Submitted (APR-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; CP015317; ARK13162.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6ECQ2; -.
DR STRING; 1834519.A6C57_24060; -.
DR KEGG; fib:A6C57_24060; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000193660; 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:UP000193660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..149
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 403..494
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 883 AA; 98785 MW; E42AACA9D475630C CRC64;
MDFKNYTIKA QEVVQQAAQI AQGNQQQTVE TGHILKAILD EDPNTVGYLA KTVGTDVSRL
DLALNAIVSG YPKVVVSGDA QQGIYLGGDL NAALQRSTSF LKEFGDEYVS VELMLLGLVG
GRDAVATLLK DVGFSEKTLK EAIKALRGKN NPVKNQNAEA TYQSLERYSI NLNDRANAGK
IDPVIGRDEE IRRVLQILSR RTKNNPILLG EPGVGKTAIV EGLAQRIVQG DVPENLKSKQ
IVSLDMGLLV AGAKYKGEFE ERLKSVIKEV TDSEGEIILF IDEIHTLVGA GGGGEGAMDA
ANLLKPALAR GELHAIGATT LKEYQKYIEK DKALERRFQA VIVDEPDVPD AISILRGIKD
KYELHHGVRI KDDAVIAAVE LSNRYISDRF LPDKAIDLMD EAAAKLRLEM DSVPEELDEL
NRRIMQLEIE REAIRRENDR DKETVLNKQI ADLSDERNEL RAKWETEKAS VNESRTAKEQ
LDQLRFEAEQ AERAGDYGKV AEIRYGRIPE LEAKLTAATQ TANNADGADR MMQEEVNAED
IAEVVAKWTG IPMSRMVQSE RDKLLFLEAE LGKRVAGQEE AIEVVADAVR RSRAGMQDPK
RPIGSFIFLG TTGVGKTELA RALADFLFND ENALVRIDMS EYQERHAVSR LIGAPPGYVG
YDEGGQLTEA VRRKPYSVIL LDEIEKAHPD VFNILLQVLD DGRLTDNKGR VANFKNTIII
MTSNIGSQII RERFSDIDTS NREQVIDQTK EEVFELLKQT VRPEFLNRID ELVMFQPLTK
REIRKIMEIQ FKQIQHRLAE QGMVLEADNE VLDFIAREGY DPVFGARPLK RVMQRRILNA
LSKEILSGRI QKNAIVGMML NEDENGQEDI IFYNLDKVVP VLD
//