ID A0A4R2BKW5_9BACI Unreviewed; 865 AA.
AC A0A4R2BKW5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=EV146_101217 {ECO:0000313|EMBL:TCN27887.1};
OS Mesobacillus foraminis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=279826 {ECO:0000313|EMBL:TCN27887.1, ECO:0000313|Proteomes:UP000295689};
RN [1] {ECO:0000313|EMBL:TCN27887.1, ECO:0000313|Proteomes:UP000295689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CV53 {ECO:0000313|EMBL:TCN27887.1,
RC ECO:0000313|Proteomes:UP000295689};
RX PubMed=26203337; DOI=.1186/s40793-015-0017-x;
RA Whitman W.B., Woyke T., Klenk H.P., Zhou Y., Lilburn T.G., Beck B.J.,
RA De Vos P., Vandamme P., Eisen J.A., Garrity G., Hugenholtz P.,
RA Kyrpides N.C.;
RT "Genomic Encyclopedia of Bacterial and Archaeal Type Strains, Phase III:
RT the genomes of soil and plant-associated and newly described type
RT strains.";
RL Stand. Genomic Sci. 10:26-26(2015).
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:TCN27887.1}.
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DR EMBL; SLVV01000001; TCN27887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R2BKW5; -.
DR Proteomes; UP000295689; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Hydrolase {ECO:0000313|EMBL:TCN27887.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:TCN27887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000295689};
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 111..138
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 415..529
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 97696 MW; E4225A507D6AD92F CRC64;
MDFNMMTERT QQAFTEAQAL AAKRSHQEVD EAHLLLAMLE LDESLAATIL ERAGERTQDY
IQALQELLNK KPEVTITGGE AGKLYITASL QRLMLAAGEE MKHFHDEYLS AEHLLLAMQK
AKTEVGELLE QKRLSREKLM SAIKEIRGNT RVTSQNPEAG YDALKKYGRD LVEEARKNRM
DPVIGRDGEI RNVIRILSRK TKNNPVLIGE PGVGKTAIVE GLAQRIIRKD VPEGLKDKTI
FALDMSSLIA GAKFRGEFEE RLKAVLNEVK KSEGKILLFI DELHTIVGAG KTEGAMDAGN
MLKPMLARGE LHCIGATTLD EHRKYIEKDP ALERRFQQVL VQEPNVEDTI SILRGLKERF
EIHHGVNIHD RAIVAAATLS DRYITDRFLP DKAIDLVDEA CAMIRTEIDS MPTELDEVTR
RIMQLEIEEA ALQKEKDEAS EDRLQALQKE LADLRDIAGT MKGKWQKEKE GIQSVQEKRE
TLEALRHQLE KAENEYDLNK AAELRHGRIP ALEKELKELE SEIGGEKEGR LLREEVTEEE
IASIVARWTG VPVTRLVEGE REKLLRLESI LHDRVIGQEE AVSLVSDAVL RARAGIKDPN
RPIGSFIFLG PTGVGKTELA KTLAEALFDS EEQMIRMDMS EYMEKHAVSR LIGAPPGYVG
YEEGGQLTEA VRRKPYSVIL LDEIEKAHPE VFNILLQMLD DGRITDSQGR TVDFKNTVII
MTSNIGSHFL LDQSAKEEGI SEEVREMAMS QLRSHFRPEF LNRVDEMILF KPLRLREIKA
IVSKLAEDLQ KRLSPQQIQI SISDEAKEFI AVNGFDPVYG ARPLKRFIQR QVETKLAREI
IAGTIREKST AEISVEGKEI TVRVK
//