ID A0A401ZSJ2_9CHLR Unreviewed; 871 AA.
AC A0A401ZSJ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB_2 {ECO:0000313|EMBL:GCE09888.1};
GN Synonyms=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=KDAU_72170 {ECO:0000313|EMBL:GCE09888.1};
OS Dictyobacter aurantiacus.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Dictyobacter.
OX NCBI_TaxID=1936993 {ECO:0000313|EMBL:GCE09888.1, ECO:0000313|Proteomes:UP000287224};
RN [1] {ECO:0000313|Proteomes:UP000287224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-27 {ECO:0000313|Proteomes:UP000287224};
RA Wang C.M., Zheng Y., Sakai Y., Toyoda A., Minakuchi Y., Abe K., Yokota A.,
RA Yabe S.;
RT "Tengunoibacter tsumagoiensis gen. nov., sp. nov., Dictyobacter kobayashii
RT sp. nov., D. alpinus sp. nov., and D. joshuensis sp. nov. and description
RT of Dictyobacteraceae fam. nov. within the order Ktedonobacterales isolated
RT from Tengu-no-mugimeshi.";
RL Submitted (DEC-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:GCE09888.1}.
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DR EMBL; BIFQ01000002; GCE09888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401ZSJ2; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000287224; 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:UP000287224};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 871 AA; 98024 MW; 558C29F9BA6D6DB5 CRC64;
MNIEHFTEKS REAVSSAAQI AREHNHNQVE VEHLLAALLA QEGGVVQQII TKAGGNLAAA
QKAINDELER MPKVYGGSEP GISPRLRKLL EDAWNEMNAF HDEYLSVEHL LLAMFNIKDG
AVPRILQAAR LTRENVLQAL TSIRGAQRVT DQNPEGKYEA LEKYGRNLTT LAQQGKLDPV
IGRDEEIRRV IQVLSRRTKN NPVLIGEPGV GKTAIVEGLA LRIVRGDVPR TLANKQIISL
DLSALVAGAK YRGEFEDRLK AVLKEVTGSE GNIILFIDEL HTLVGAGAAE GAMDASNMLK
PMLARGELHC IGATTLDEYR KHIEKDAALE RRFQPIIVEP PSVEDTISIL RGLKQRYEIH
HGVRITDGAI VAAAVLSDRY ITDRFLPDKA IDLIDEAASR LRVELDSTPT EIDALDRRIR
QLQVELEALK KETDEASKER LTRVTQEITS LQEQLDALEQ AFERERAPVE TIQRLTKELE
QAQVELERAE REYNFEKAAE LRHGTIPKLE QQITETEAQL SNIKGKRLLK EEVDAEDIAE
VVAKWTHIPV SRLMEGEIEK LVHMEERLRL RVVGQELALT AVSNAIRRAR AGLQDPHRPL
ASFLFLGPTG VGKTELARAL AEFLFDDERA IIRIDMSEYM EKYSVSRLIG APPGYVGYEE
GGQLTEAARR RPYSVVLFDE IEKAAPEVFN TLLQLLDDGR LTDGQGRTVD FKNTVIIMTS
NVGVDWLKEL ERLDEDEVQR QVRQRLRSEG FRPEFINRID EIVVFHPITR TLMKDIVTIQ
LNRLRPRLAD RHITLRVTDA ALDLLARIGY DPQFGARTLK RVIQREIENR IASDILNGTI
HDGDTIKIDA RNSKIVIEVV QSQAQQATYA T
//