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Database: UniProt
Entry: A0A4Y8I2V9_9BACT
LinkDB: A0A4Y8I2V9_9BACT
Original site: A0A4Y8I2V9_9BACT 
ID   A0A4Y8I2V9_9BACT        Unreviewed;       868 AA.
AC   A0A4Y8I2V9;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-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:TFB10332.1};
GN   ORFNames=E3V36_04200 {ECO:0000313|EMBL:TFB10332.1};
OS   Candidatus Marinimicrobia bacterium MT.SAG.2.
OC   Bacteria; Candidatus Marinimicrobia.
OX   NCBI_TaxID=2552983 {ECO:0000313|EMBL:TFB10332.1, ECO:0000313|Proteomes:UP000298410};
RN   [1] {ECO:0000313|EMBL:TFB10332.1, ECO:0000313|Proteomes:UP000298410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MT.SAG.2 {ECO:0000313|EMBL:TFB10332.1};
RA   Peoples L.M.;
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TFB10332.1, ECO:0000313|Proteomes:UP000298410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MT.SAG.2 {ECO:0000313|EMBL:TFB10332.1};
RA   Bartlett D.H., Eloe-Fadrosh E.A.;
RT   "Metabolic potential of hadal sediment consortia and uncharacterized deep-
RT   ocean lineages.";
RL   Submitted (MAY-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:TFB10332.1}.
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DR   EMBL; SORU01000012; TFB10332.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Y8I2V9; -.
DR   Proteomes; UP000298410; 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:UP000298410};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          400..540
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   868 AA;  97321 MW;  C5E6C03675B6CDAE CRC64;
     MSFDKFTIRA QESFRRAQEL AAEFRNPELK SGHLLMAMLT DEKNTAIAII SKLGISVKEV
     NESIEGVLSK LPKATGGGIG EPQLSKELDG IINSALEESK ALKDEYISNE HLIIAMAESN
     SSSVKSELNR LGITKESILS VLQDIRGSQR VTDQNPEDKY QALERYGKDL NELARLNKLD
     PVIGREEEIR RIMQILSRRS KNNPVLIGDP GVGKTAIVEG LAFRIVKSDV PDGMKDKRIV
     ALDMGSLLAG AKFRGEFEER LKAVIKEVED SNGEVILFID ELHTVVGAGA AEGAVDASNI
     LKPSLARGEL KVIGATTIDE YRKYIEKDAA LERRFQPNYI AEPSIEDAIS IMRGLRERYE
     IHHGIKIKDS ALVAPVNLSH RYIPDRFLPD KAIDLIDEAA SKLRIDIDSM PAELDELERK
     IKQLEIEKAA ISKEEDSNKR VKEIEDQLKK IVKEAEALRG QWTAEKVAIG RLREVKEEIE
     KTRTAYDAAE LESDYEKAAE LKHGKLVELK LTEEKLEENL KKLQKGKRLL KEEIDETDIA
     GIVAQWTNIP VTRMMEGERD KLLQMEERLK ERVIGQQEAI KAVSDAVKRS RAGLQDESRP
     LGSFIFIGST GVGKTELAKG LAEFLFDDEN AMIRIDMSEY MEKHSVSRLI GAPPGYVGYE
     EGGQLTEAVR RKPYSVILLD EIEKAHHDVF NVLLQVLDDG RMTDGQGRVV NFRNTIIIMT
     SNLGSSLVVE KSEKINPENE AEIYEEIKSE INKMLQSNFR PEFLNRIDDI IVFHPLTPEN
     VKEIVNLQLK ELIGKVDEKG MKLELSDDAI LLLAEKGYEP AYGARPLKRL LQKEITDRIA
     NLLLSGEAKE GDRLDVRVNG SGLEVLID
//
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