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Database: UniProt
Entry: A0A2W2FQH9_9ACTN
LinkDB: A0A2W2FQH9_9ACTN
Original site: A0A2W2FQH9_9ACTN 
ID   A0A2W2FQH9_9ACTN        Unreviewed;       864 AA.
AC   A0A2W2FQH9;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:PZG24107.1};
GN   ORFNames=C1I98_35845 {ECO:0000313|EMBL:PZG24107.1};
OS   Spongiactinospora gelatinilytica.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Spongiactinospora.
OX   NCBI_TaxID=2666298 {ECO:0000313|EMBL:PZG24107.1, ECO:0000313|Proteomes:UP000248544};
RN   [1] {ECO:0000313|EMBL:PZG24107.1, ECO:0000313|Proteomes:UP000248544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7K107 {ECO:0000313|EMBL:PZG24107.1,
RC   ECO:0000313|Proteomes:UP000248544};
RA   Sahin N., Saygin H., Ay H.;
RT   "Draft genome sequence of Sphaerisporangium sp. 7K107.";
RL   Submitted (JAN-2018) 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:PZG24107.1}.
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DR   EMBL; POUA01000508; PZG24107.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W2FQH9; -.
DR   Proteomes; UP000248544; 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          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   864 AA;  94290 MW;  CC61359FFC4755C9 CRC64;
     MDYKLTRKSQ EAISASIRRA ATEGNPEVAP AHLFTALLAQ SGGTAVPLLE AVGADWKKLR
     TAAEQQLEGL PKAQGATVSA PTTSRALLVV LNTAAARAKQ LEDEYVSTEH LLVGLAADGG
     PIAELLKSQG ATAAALLDAF EKVRGHARVT SETPEDTYQA LEKYGVDLTE RARAGRLDPV
     IGRDAEIRRV VQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QRIVAGDVPE SLRNKRLVSL
     DLSAMVAGAK FRGEFEERLK AVLAEIKESD GQVVTFIDEL HTVVGAGAAE GSMDAGNMLK
     PMLARGELRM IGATTLDEYR ERIEKDPALE RRFQQVYVGE PSVEDTIAIL RGLKGRYEAH
     HQVQIADSAL VAAAALSDRY ITARFLPDKA IDLVDEAASR LRMEIDSRPV EIDELQRTVD
     RMKMEEMALA KETDEASRAR LDKLRKDLAD RQEELNGLVG RWEREKAGLN HVGDLKKQLD
     EARGAAERAQ RDGDFEAASR LMYAEVPRLE KELQAAVAQA QPEAAMVKEE VGPDDIAQVI
     SSWTGIPAGR LLEGETAKLL RMEDELGKRL IGQAPAVQAV SDAVRRARAG ISDPDRPTGS
     FLFLGPTGVG KTELAKALAE FLFDDERAMT RIDMSEYSEK HAVARLVGAP PGYVGYEEGG
     QLTEAVRRRP YTVVLLDEVE KAHTEVFDIL LQVLDDGRLT DGQGRTVDFR NTILIMTSNI
     GSQYLVDPTL ENGAKRDAVM NAVRASFKPE FINRLDDIIL FDALGSEELS RIVDLQAVRL
     ARRLADRRLT LTVTPAARDW LALTGYDPLY GARPLRRLVQ SAIGDRLAKK VLSGEIQDGD
     EVVVDLDEAG DTLSIEAQRS PVAQ
//
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