ID A0A1U7MGK9_9FIRM Unreviewed; 868 AA.
AC A0A1U7MGK9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB1 {ECO:0000313|EMBL:OLS56555.1};
GN Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SPSPH_00430 {ECO:0000313|EMBL:OLS56555.1};
OS Sporomusa sphaeroides DSM 2875.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1337886 {ECO:0000313|EMBL:OLS56555.1, ECO:0000313|Proteomes:UP000186950};
RN [1] {ECO:0000313|EMBL:OLS56555.1, ECO:0000313|Proteomes:UP000186950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2875 {ECO:0000313|EMBL:OLS56555.1,
RC ECO:0000313|Proteomes:UP000186950};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa sphaeroides DSM 2875.";
RL Submitted (FEB-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}.
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:OLS56555.1}.
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; LSLJ01000001; OLS56555.1; -; Genomic_DNA.
DR RefSeq; WP_075752144.1; NZ_LSLJ01000001.1.
DR AlphaFoldDB; A0A1U7MGK9; -.
DR STRING; 1337886.SPSPH_00430; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000186950; 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:UP000186950};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..493
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 868 AA; 96927 MW; F321851E9459132F CRC64;
MNNEKYTQKA AAALQESQQL AALHYHQELT TRHLALALIK DAVGITAYLL AQLQIDVRML
TAKLEQLLKT LPSVRGQDGG LRMNTAMIRV LALAEKQANA MKDEYISVEH LLIAIAEDGD
SDVVAACRDF GLTKGKILET VNQFRRGQSI TSDNPDENLQ ALNKYGRDLT ELAKAGKLDP
VIGRDEEIRR VVEILSRRTK NNPVLIGEPG VGKTAIVEGL ARRIIAGDVP ESLKNKTVYS
LDLGAMVAGA KFRGEFEERL KTVLSEITKA EGKIILFIDE LHTVVGAGAA EGAMDAGNIL
KPMLARGELK CIGATTLNEY RKHIEKDAAL ERRFQPIMVD QPGTEDTISI LRGLRERYEV
HHGVKIKDAA LVAAAVLSDR YIADRFLPDK AIDLVDEAAA KLRTEIDSMP SELDEALRRI
MQLEIEEQAL KKETDTASKD RLERIHHELA SLKEQADSLK AQWQLEKQAI VRLREVKEEI
ETVRTQMEAA ERSYDLNRLA ELKYGRLPEL EKKLKTEEER LTQNRSHKAM LKEEVDEDDI
AKVVSRWTGV PVTKLMTGER EKLVNLESVL HHRVIGQDTA VTAISEAIIR ARAGIKDPGR
PIGSFIFLGP TGVGKTELAK TLAEVLFDDE RSMIRLDMSE YMEKHAVARL IGAPPGYVGY
DEGGQLTEAV RRRPYSVLLL DEVEKAHNDV FNVLLQILDD GRLTDSKGRT VDFKNTVIIM
TSNLGSHEIL NNEFAAAKER VLELLKHHFR PEFLNRIDDI IVFNALTAAQ VAEIAAIMLE
NLNKRLHKQL NISLAWDDNA LELLANEGYD PQFGARPLKR LISQLVETEL SKMIIRSEIQ
ENSKVTLHAP AGKLVFTVEP KVTTASQD
//