ID A0A1T4WQI3_9BACT Unreviewed; 861 AA.
AC A0A1T4WQI3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN02745166_00516 {ECO:0000313|EMBL:SKA79614.1};
OS Prosthecobacter debontii.
OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales;
OC Verrucomicrobiaceae; Prosthecobacter.
OX NCBI_TaxID=48467 {ECO:0000313|EMBL:SKA79614.1, ECO:0000313|Proteomes:UP000190774};
RN [1] {ECO:0000313|EMBL:SKA79614.1, ECO:0000313|Proteomes:UP000190774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700200 {ECO:0000313|EMBL:SKA79614.1,
RC ECO:0000313|Proteomes:UP000190774};
RA Peterson S.W.;
RL Submitted (FEB-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; FUYE01000002; SKA79614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4WQI3; -.
DR STRING; 48467.SAMN02745166_00516; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000190774; 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 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 Hydrolase {ECO:0000313|EMBL:SKA79614.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SKA79614.1};
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 415..502
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 96066 MW; 70A8C274C57B4B33 CRC64;
MSPEKFTVKL QEAFNASQSV ATRHGHQELK PAHLLTALLD QEGGITRPLF EKAAVNPAAV
ANLSTQLANL LSRQPKVSGA TGSLYLSNEF RELMTKAEDE QKKLKDDFLS VEHVLLALFK
IKSDVADLLK QAGLTYDTVS KGLAAVRGSQ RVTDQDPEGK YQTLEKYGTD LTARARQGKI
DPVIGRDEEI RRVMQVLSRR SKNNPVLIGE PGVGKTAIAE GLARRIVAGD VPDSLKGKRL
ISMDLGGMMA GAKFRGEFEE RLKAFLKEVT SSEGEIILFI DELHTIVGAG KAEGAMDAGN
LLKPQLARGE LRCIGATTLD EYRKYIEKDP ALERRFQPVM VGEPSVEDTI AILRGLKERY
EVHHGVRIQD GAIIAAATLS NRYITDRFLP DKAIDLVDEA ASRIKIELDS MPTEIDVIER
EIMQHEMQRQ VLKKEKDAAS LARLEKLEKE IADLKEQSGA LKAQWLKEKE AVDAGRKVKE
EIDRLRTELE QAQRRGDFAR AGEIQYGLIP DLEKKLQNEP NQTQAPAPKP TLLREEVTEE
DIARVVANWT GIPVSRLQEG ERSKLVKMEE RLAARVIGQK DAIVAVSNAV RRARAGIQDE
NRPIGSFLFL GPTGVGKTEL CKALAEFLFD DENAMTRLDM SEYMEKHSVS RLIGAPPGYV
GYDEGGQLTE AVRRRPYSVV LFDEVEKAHP DVFNTLLQVL DDGRITDGQG RTVDFKNTVI
IMTSNIGSQH IQDVQNPEQR EALVRDSLKQ FFRPEFLNRI DEIVIFDRLN ANELDKIVKI
QLQRVIDRLA KQNIHLTVSD DTTRYLADAG FDPVFGARPL KRAIQKHLLD PLSLAVLEGN
FKEGDHIDAV LKDGRVEFVK A
//
