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Database: UniProt
Entry: A0A177LCJ9_9BACI
LinkDB: A0A177LCJ9_9BACI
Original site: A0A177LCJ9_9BACI 
ID   A0A177LCJ9_9BACI        Unreviewed;       861 AA.
AC   A0A177LCJ9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AWH49_00215 {ECO:0000313|EMBL:OAH63313.1};
OS   Domibacillus aminovorans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX   NCBI_TaxID=29332 {ECO:0000313|EMBL:OAH63313.1, ECO:0000313|Proteomes:UP000076935};
RN   [1] {ECO:0000313|EMBL:OAH63313.1, ECO:0000313|Proteomes:UP000076935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1314 {ECO:0000313|EMBL:OAH63313.1,
RC   ECO:0000313|Proteomes:UP000076935};
RA   Verma A., Pal Y., Krishnamurthi S.;
RT   "Investigation of taxonomic status of Bacillus aminovorans.";
RL   Submitted (JAN-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:OAH63313.1}.
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DR   EMBL; LQWY01000001; OAH63313.1; -; Genomic_DNA.
DR   RefSeq; WP_063964279.1; NZ_LQWY01000001.1.
DR   AlphaFoldDB; A0A177LCJ9; -.
DR   STRING; 29332.AWH48_14940; -.
DR   Proteomes; UP000076935; 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   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..500
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   861 AA;  96399 MW;  0B661874415814CE CRC64;
     MKMDNMTYTM QEALAAAQQS AVERNHSDVD TVHMMIALTS KEDGLFSRIL ERAGMKRAVL
     LRVLQQAIQT KPVVSGDAQY GAYLSSGLNT WFQKATSIQK EFDDAYLSVE HMTATIFSAG
     KVIADVLKKE HVTEKAILNA IHEIRGNEKV TTQNPEAGYE ALAKYGRDLV EEVRAGKIDP
     VIGRDDEIRH VIRILSRKTK NNPVLIGEPG TGKTAIVEGL AWRIVRKDVP DGLKDKTIFS
     LDMSSLIAGA KFRGEFEERL QAVLNEVKKS EGNILLFIDE IHTIVGAGKT EGSMDAGNML
     KPMLARGELH CIGATTLDEH RQYIEKDPAL ERRFQPVLVS EPTIEDTISI LRGLKERFEI
     HHGVNIHDRA LVAAATLSNR YITDRFLPDK AIDLMDEACA MIRTEIDSMP TELDAVMRRV
     MQLEIEEAAL RKEKDAESAA RLVHIQKELS NLKEQADTMK AQWMGEKEAI MHVKEKRGEL
     DRLRRELEDA ESRYDLNRAA ELRHGQIPAV EKELVDLEAG AADEKENRLL REEVTEEEIA
     SIVARWTGIP VTKLVEGERE KLLRLEDILH ERVIGQDEAV SLVSDAVLRA RAGIKDPNRP
     IGSFLFLGPT GVGKTELAKT LADVLFDSEE QMIRLDMSEY MEKHSVSRLV GAPPGYVGYE
     EGGQLTEAIR RRPYSVVLLD EVEKAHPDVF NILLQILDDG RITDSQGRMV DCKNTVFIMT
     SNIGSSHLLE MGSEGEIPEE AKNNVMMQLR AHFRPEFLNR VDDIVLFKPL TRDNLKDIAS
     KILVGLDERL ADRGITLSVT DEAKDIIVEE GYDPVFGARP LKRFIQRQIE TKVARSIIAG
     EILPGATAVV DVKEGELVVR K
//
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