ID A0A4Q1B1E5_9STAP Unreviewed; 862 AA.
AC A0A4Q1B1E5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:RXK18747.1};
GN ORFNames=ER639_00115 {ECO:0000313|EMBL:RXK18747.1};
OS Macrococcus sp. DPC7161.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae; Macrococcus.
OX NCBI_TaxID=2507060 {ECO:0000313|EMBL:RXK18747.1, ECO:0000313|Proteomes:UP000293889};
RN [1] {ECO:0000313|EMBL:RXK18747.1, ECO:0000313|Proteomes:UP000293889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC7161 {ECO:0000313|EMBL:RXK18747.1,
RC ECO:0000313|Proteomes:UP000293889};
RA Mazhar S., Altermann E., Hill C., Mcauliffe O.;
RT "Macrococcus lingua sp. nov., from bovine tongue.";
RL Submitted (JAN-2019) 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:RXK18747.1}.
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DR EMBL; SDSC01000001; RXK18747.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Q1B1E5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000293889; 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:UP000293889};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251};
KW Stress response {ECO:0000256|ARBA:ARBA00023016,
KW ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 50..113
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 411..498
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 98034 MW; 71DBC68D36D3ED4D CRC64;
MNLDQMTYNV QNAIQFAQNE AVEMKQQQIE TEHLIKHFLV NSDNMLQTVF ERANIDIKQY
ETLIQQALQK YPQVEGENIQ YGSYLSQNLN TVLNEANQQM KTFEDEYVSV EHIIMALITK
HTLTKDFIGN KQDVIKEIIM NIRGGNKVTT QNPEVQYEVL KKYGRDLVEE VKKGKMDPVI
GRDEEIRNTI RILSRKTKNN PVLIGEPGVG KTAIVEGLAQ RIVKKDVPDS LLNKTIFELD
LSALVAGAKF RGEFEERLKA VLKEVKESNG EIILFIDEIH MLVGAGKTDG AMDAGNMLKP
MLARGELHCI GATTLNEYRE YIEKDSALER RFQKVLVKEP DLEDTISILR GLKERYEVHH
GVRIQDNALV AAAELSDRYI TDRFLPDKAI DLVDQACATI RTEMGSNPTE LDAVNRRVLQ
LEIEEKALKS EKDARSKSRL EELQRELANE KEKQQQLNAR VEKEKGQIAI VQEKRAELDR
LRKQLEEAQT NYDLAKASEL QYGAIPKIEK ELTELENNLI EETKGTDRLI REVVTEEEIG
YIVSQWTGIP VSKLVETEKE KLLKLSDILH ERVVGQDEAV DLVADAVVRA RAGIKDPNRP
IGSFLFLGPT GVGKTELAKT LASTMFDSEK HMIRIDMSEY MEKHAVARLI GAPPGYVGYE
EGGQLTEAVR RNPYSVILLD EVEKAHSDVF NVLLQLLDEG RLTDSKGRVV DFKNTIIIMT
SNIGSQYLLD GIQNDEITNK ARKLVMDSLH AYFKPEILNR MDDIVLFKPL SANDMTYIVD
KLIMQLNMRL MDQHLEVKVS DEVKHWVAKE AYEPQFGARP LKRFVQRHIE TPLARNIIRE
GYPEGTVIEV GLSDNGVTFN VM
//