GenomeNet

Database: UniProt
Entry: A0A4Q1B1E5_9STAP
LinkDB: A0A4Q1B1E5_9STAP
Original site: A0A4Q1B1E5_9STAP 
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}.
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; 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
//
DBGET integrated database retrieval system