ID A0A401ZUP5_9CHLR Unreviewed; 862 AA.
AC A0A401ZUP5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:GCE10639.1};
GN ORFNames=KTT_04980 {ECO:0000313|EMBL:GCE10639.1};
OS Tengunoibacter tsumagoiensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Dictyobacteraceae; Tengunoibacter.
OX NCBI_TaxID=2014871 {ECO:0000313|EMBL:GCE10639.1, ECO:0000313|Proteomes:UP000287352};
RN [1] {ECO:0000313|Proteomes:UP000287352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Uno3 {ECO:0000313|Proteomes:UP000287352};
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:GCE10639.1}.
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DR EMBL; BIFR01000001; GCE10639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401ZUP5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000287352; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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 InterPro; IPR002078; Sigma_54_int.
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.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 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:UP000287352};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT DOMAIN 571..827
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT COILED 404..525
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 862 AA; 97266 MW; FC38151F5490DACA CRC64;
MKIERFTDKA RDAVQDAAEL ARKHNHSQIE PEHLLAALLT QENGVVPQVI QKAGGNVATV
RRNIDSELEK MSRVYGGSEP GISPRLRKVL EDAWNEMNQF KDEYLSVEHM LLAFFENDSA
AQRVLKSAGL TRDVTLQALT AIRGSQRITD PNPEGKYQAL ERYGRNLTEL AQQGKLDPVI
GRDEEIRRVI QVLSRRTKNN PVLIGEPGVG KTAIVEGLAQ RIVRGDVPKS LANKQVITLD
LGALVAGAKF RGEFEERLTA VLKEVIGAEG GIILFIDELH TLVGAGASEG AMDASNMLKP
MLARGELHCI GATTLDEYRK YIEKDAALER RFQPVIVDQP TVEDTISILR GLKPRYEVHH
GVRIQDSALV AAAVLSNRYI TDRFLPDKAI DLVDEAASLR RVELDSTPSE LDALERRIRQ
LQVEQQALKK ETDAASRERL EKVERELANL NEQLHSLKLT LEGERAPVEE LRKLKKQLEE
AQVAYEKAER AYDYDTMARL SYGTIKQLEQ QIKDQEARLV NLQTSRMLKE EVDAEDIAEI
VSKWTHIPLS RLMEAEVKKL LTMEDRLRER VVGQNTALEI VSDAVRRSRA GLQDPNRPLA
SFLFLGPTGV GKTELARALA EFLFDNEQAM VRIDMSEYME KHSVSRLIGA PPGYVGYDEG
GQLTEAVRRR PYSVILLDEI EKAAPEVFNI LLQILDDGRL TDGQGRTIDF KNTVIIMTSN
VGDRWIHEYE GMDEDDVQRN IRQRLREEGF RPEFINRIDE VIIFHPISRD KVKDIVEIQI
NRLRPRLEER NITLNLTEAA KNYLAEEGYD PQFGARPLKR VIQREVENRI ARGLLDGSII
DGSTVTIDEQ DGKLTPVTSP NV
//