ID A0A1F7BPD6_9BACT Unreviewed; 854 AA.
AC A0A1F7BPD6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=A2635_03530 {ECO:0000313|EMBL:OGJ59391.1};
OS Candidatus Peribacteria bacterium RIFCSPHIGHO2_01_FULL_51_9.
OC Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria.
OX NCBI_TaxID=1801915 {ECO:0000313|EMBL:OGJ59391.1, ECO:0000313|Proteomes:UP000179204};
RN [1] {ECO:0000313|EMBL:OGJ59391.1, ECO:0000313|Proteomes:UP000179204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGJ59391.1}.
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DR EMBL; MFXQ01000018; OGJ59391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F7BPD6; -.
DR Proteomes; UP000179204; 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 78, MITOCHONDRIAL; 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 Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..141
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 407..487
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 854 AA; 95619 MW; 20522CD045CD65A1 CRC64;
MDFNHYTTKA SEAIQGTMQL AGKLNHQALT PLHLMLVLIE QQGGLVPTLL QKGEQDPETL
AEKIQKELAT LPTVSGGTQA YLTQELRKVL EQAESDAGKM RDEYISTEHL LLALLDDKSI
QSVLRVPKKD ILTALQSLRG NQHVTDQDPE GKYQALEKYT QDFTRLAQEG KVDPVIGRDE
EIRRIMQILS RRTKNNPVLV GEPGTGKTAI VEGLAKKIVD GDVPDPLKGK KVLALDLGAL
IAGTKYRGEF EDRLKAVIKE IENSEGQIIL FIDELHTIVG AGGAEGAMDA GNLLKPALAR
GKLHTIGATT LKEYRKYIEK DAAFERRFQQ VSVEPPSVKD AISILRGIKE KYEVHHGVRI
QDPAIVAAVT LSDRYIADRF LPDKAIDLMD EAAATLRIEM DSKPTELDQL DRQIRQLEVE
KEALKKEKDE ASKKRLHTIE KELSELRERQ KELDVRWQNE KKIIDVLKAA GKEIDAYKAE
AQQTERSGNL QRVAEIRYGL IPDCEKRITS SQKELAKIQK GNAILKEEVT EEDIARIVAR
WTGIPVQKML QEETDKLAHM EQEIGKRIVG QEEAIKAISN AVRRSRAGIQ EGGRPIGTFI
FLGPTGVGKT ELAKALAEFL FNNEGLITRI DMSEYMEKHA IARLIGSPPG YVGYEEGGQL
TEAVRRHPYT VILFDEIEKA HPDVFNILLQ ILDEGRLTDS KGRTVDFTNT VIIMTSNLGS
DEIAKHAGEK ILQTKAIDSL LRQTFRPEFL NRIDEIIVFQ PLSQDQIARI VTLQIAHLKK
RLEQKGISIT LTDKASEYLA ARGFDQIFGA RPLKRVIQNE ILDPLSLEII EGKLKEGNTV
KLDVKDGKIV FEKK
//
