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
//