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Database: UniProt
Entry: A0A4Q4ZA11_9ACTN
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ID   A0A4Q4ZA11_9ACTN        Unreviewed;       878 AA.
AC   A0A4Q4ZA11;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RYP84438.1};
GN   ORFNames=EKO23_15550 {ECO:0000313|EMBL:RYP84438.1};
OS   Nocardioides guangzhouensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=2497878 {ECO:0000313|EMBL:RYP84438.1, ECO:0000313|Proteomes:UP000295198};
RN   [1] {ECO:0000313|EMBL:RYP84438.1, ECO:0000313|Proteomes:UP000295198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130 {ECO:0000313|EMBL:RYP84438.1,
RC   ECO:0000313|Proteomes:UP000295198};
RA   Fu Y., Cai Y., Lin Z., Chen P.;
RT   "Nocardioides guangzhouensis sp. nov., an actinobacterium isolated from
RT   soil.";
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:RYP84438.1}.
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DR   EMBL; SDKM01000023; RYP84438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Q4ZA11; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000295198; 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:UP000295198};
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          87..114
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
FT   COILED          417..504
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   878 AA;  96935 MW;  5D1D91A3F55E6039 CRC64;
     MDMNRLTQKS QEALHDAQTK ALRFGHVEVD GEHLLLALLD QAEGLVAPLL ARAGADPGRL
     REELEAELGR RPRVTGPGVT PGQVHITQRL SRLLDTADRE ARRLKDEYVS VEHLVIALVE
     EGSGSAAGRL LHAQGLTRDT FLAALTEVRG HQRVTSATPE GTYEALEKYG RDLVAAAEAG
     KLEPVIGRDS EIRRTVQILS RKSKNNPVLI GEPGVGKTAI VEGLAQRIAD GDVPEGLRDK
     TVFALDLGAL IAGAKYRGEF EERLKAVLNE VQSAEGHILL FVDELHTVVG AGAAEGAMDA
     GNMLKPLLAR GELHMIGATT LDEYRTHIEK DAALERRFQP VLVDEPDEED ALSILRGLRE
     RLEVFHGVKI HDGALVAAVT LSHRYISDRF LPDKAIDLVD EACAMLRTEI DSMPAELDEL
     TRRVTRMEIE EAALSEEEDA ASRARLEELR KELADARAET DALRAQWEAE RSALREVQSL
     RQELEQVRLE SERAEREYDL NRAASLRHGQ LPEIQRRLEA AESRLAGKQG GRRLLREVVT
     ADEIADIVSR WTGIPVTRLQ EGERDKLLRL DEVLHERVIG QDEAVQLVAD AVVRARSGIK
     NPQRPIGSFI FLGPTGVGKT ELAKTLAAAL FDTEENMVRI DMSEYQERHT VSRLVGAPPG
     YVGFEEGGQL TEAVRRKPYS VVLLDEIEKA HVDVFNTLLQ VLDDGRLTDS HGRTVDFRNT
     VLIMTSNIGS EYLLEGVTAG GEVKDDARSM VMRTLQSHFR PEFLNRVDEI VMFKPLTLAE
     IERIVDLQLE ELHERLADMR ITLEVTAAAR RFIADQGFDP AYGARPLRRL ISREVETQVG
     RALLRGDAAD GGAISVDVAD GKIMVTAAGN PSEGRAVA
//
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