ID W2EUK4_9ACTN Unreviewed; 872 AA.
AC W2EUK4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=MPTA5024_14790 {ECO:0000313|EMBL:ETK35315.1};
OS Microbispora sp. ATCC PTA-5024.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Microbispora.
OX NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK35315.1, ECO:0000313|Proteomes:UP000018869};
RN [1] {ECO:0000313|EMBL:ETK35315.1, ECO:0000313|Proteomes:UP000018869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK35315.1,
RC ECO:0000313|Proteomes:UP000018869};
RX PubMed=24459268;
RA Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA Stegmann E., Weber T.;
RT "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT Producing the Lantibiotic NAI-107.";
RL Genome Announc. 2:e01198-13(2014).
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|ARBA:ARBA00004496,
CC 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:ETK35315.1}.
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DR EMBL; AWEV01000108; ETK35315.1; -; Genomic_DNA.
DR RefSeq; WP_036324502.1; NZ_KI866523.1.
DR AlphaFoldDB; W2EUK4; -.
DR STRING; 316330.MPTA5024_14790; -.
DR PATRIC; fig|316330.3.peg.2866; -.
DR HOGENOM; CLU_005070_4_1_11; -.
DR OrthoDB; 3170949at2; -.
DR Proteomes; UP000018869; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 78, MITOCHONDRIAL; 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 Hydrolase {ECO:0000313|EMBL:ETK35315.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ETK35315.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018869};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..151
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 410..531
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 872 AA; 97185 MW; 118FB754DE17FFA7 CRC64;
MDLNRLTQKS QEALHDAQTA ALRFGHTEVD GEHLLLALIR QPDGLVPRLL SVAGGDPDKL
QLELEHELER RPRATGPGAA PGQVYVTQRL SQLFDAAERE AGRLKDEYVS VEHLLLALLD
EGADSAAGRL LKGHGLTRER FLSVLTQVRG NQRVTSANPE VAYEALEKYG RDLVAAARAD
KLDPVIGRDG EIRRVVQILS RKSKNNPVLI GDPGVGKTAI VEGLAQRIAR GDVPEGLKDK
TIFSLDMGAL VAGAKYRGEF EERLKAVLTE VTASEGRILL FVDEVHTVVG AGAAEGAMDA
GNMLKPLLAR GELHLIGATT VAEYRKHIEK DAALERRFQP VFVDEPSVED SISILRGLRE
RLEVFHGVKI QDGAIVAAVV LSHRYISDRF LPDKAIDLVD EACAMLRTEI DSMPAELDEL
TRRVMRLEIE EAALAKEDDP ASRERLETLR KELADLRAEA DAMRAQWEAE RHALRKVQQL
RQEIESVRRE AEQAERVYDL NRAAELRHGR LPELERKLRA AEEQLESKQG GQRLLREVVT
EEEIAGIVSR WTGIPVSRLR EGEREKLLRL DEILHRRVIG QDEAVQAVAD AIIRARSGIK
DPRRPIGSFI FLGPTGVGKT ELAKALAAAL FDTEDNIVRV DMSEYQERHT VSRLVGAPPG
YVGYEEGGQL TEAVRRKPYS VVLFDEIEKA HSDVFNTLLQ VLDDGRLTDA QGRTTDFRNT
VIIMTSNIGS HYLTEKAAPS GEIDPEVREM VMAELRARFR PEFLNRIDDI VLFKPLTETE
IEQIVKLMFN DIRARLAERR MTLEISPEAV RCIAERGFDP IYGARPLRRF ISREVETRIA
RALVAGDVRD GATIRVGLSG GEIVVTYDNP EG
//
