ID A0A1W2GZ23_9BACT Unreviewed; 870 AA.
AC A0A1W2GZ23;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN00777080_0395 {ECO:0000313|EMBL:SMD41861.1};
OS Aquiflexum balticum DSM 16537.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Aquiflexum.
OX NCBI_TaxID=758820 {ECO:0000313|EMBL:SMD41861.1, ECO:0000313|Proteomes:UP000192333};
RN [1] {ECO:0000313|EMBL:SMD41861.1, ECO:0000313|Proteomes:UP000192333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16537 {ECO:0000313|EMBL:SMD41861.1,
RC ECO:0000313|Proteomes:UP000192333};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; LT838813; SMD41861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2GZ23; -.
DR STRING; 758820.SAMN00777080_0395; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000192333; Chromosome i.
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:SMD41861.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SMD41861.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192333};
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 397..522
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 870 AA; 98222 MW; 793EF3D05165F56F CRC64;
MDFKQFTIKS QEAIQKAVEL TSAEQQQVIE PAHLLKGIFS EDENVTDFLF KKLGVNKGLI
IQKTDEIISN YPKVSGQQPY LSNAANQVLS KAKDYLKNFG DEFIAIEHLL LAILAGSEKT
AQLLKDQGMS EKPLIEAIKE LRKGNKVTDQ NAESKYRALE KYSKNLNELA KKGKIDPVIG
RDEEIRRVLQ ILARRTKNNP ILLGEPGVGK TAIVEGLAQR IISGDVPENL KSKILISLDM
GLLVAGAKYK GEFEERLKAV IKEVTDSEGE IILFIDEIHT LIGAGGGGEG AMDAANLLKP
ALARGELHAI GATTLKEYQK YIEKDKALER RFQAVMVNEP DSADAISILR GIKDKYELHH
GVRIKDDAVI AAVELSQRYI SDRFLPDKAI DLMDEAAAKL RMEIDSLPQE LDELNRRIMQ
LEIEREAIRR ENNKDKETVL SKEIAELSEK RQNVKAKWES EKAVITGIRT EKESIDRLKL
EAEQAERAGD FGKVAEIRYG KIVEAEQKLD KYKSQLEEMQ QGSPLLKEEV DNEDIAAVVS
KWTGIPLSKM IQSEREKLLH LEDELGKRVA GQREAITAIS DAVRRSRAGL QDPKRPIGSF
IFMGTTGVGK TELAKALAEY LFNDENSMVR IDMSEYQERH AVSRLVGAPP GYVGYDEGGQ
LTEAVRRKPY SVVLLDEIEK AHPDVFNILL QVLDDGRLTD NKGRIANFKN TIIILTTNIG
SHLIQERFAE MEEWNKEEIL EKTKSEVYDL LKKSVRPEFL NRIDETIMFE PLNRKVIRKI
VDIQWREIQQ RLAESNIEIE ATQEVLDFLG QVGFDPQFGA RPLKRTMQRL ILNELSKQIL
SGYIKNDSAV LVDLDAENQV YFKNIESVEV
//