ID A0A0B0EI07_9BACT Unreviewed; 863 AA.
AC A0A0B0EI07;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SCABRO_03962 {ECO:0000313|EMBL:KHE90310.1};
OS Candidatus Scalindua brodae.
OC Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC Candidatus Scalinduaceae; Scalindua.
OX NCBI_TaxID=237368 {ECO:0000313|EMBL:KHE90310.1, ECO:0000313|Proteomes:UP000030652};
RN [1] {ECO:0000313|EMBL:KHE90310.1, ECO:0000313|Proteomes:UP000030652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU1 {ECO:0000313|EMBL:KHE90310.1};
RA Speth D.R., Russ L., Kartal B., Op den Camp H.J., Dutilh B.E., Jetten M.S.;
RT "Draft genome of anammox bacterium scalindua brodae, obtained using
RT differential coverage binning of sequence data from two enrichment
RT reactors.";
RL Submitted (OCT-2014) 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:KHE90310.1}.
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DR EMBL; JRYO01000268; KHE90310.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0EI07; -.
DR PATRIC; fig|237368.3.peg.4262; -.
DR eggNOG; COG0542; Bacteria.
DR Proteomes; UP000030652; 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..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 405..526
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 863 AA; 97092 MW; 33DFD0122F2F227D CRC64;
MRLDKFTIKA QDAIQEAQQF AGSKGHQQVE SLHLLVSLLQ QQQGVVVPIM KKLGVNSDEV
LAKAHKAVDL LPQVSGAQGQ YISNELKDIL NKATVEAGRL KDEYVSTEHL LISLADNKQN
AAGKILLESG VRSTDIFTAL KGIRGNQRIT DQNPEEKYQA LERYCKDLVE LASKGKLDPV
IGRDDEIRRV IQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVDGDVPE GLRNKRVRSL
DMGALIAGAK FRGEFEDRLK AVLKDIDASE GQSILFIDEL HTVVGAGAAE GAVDASNLLK
PALARGELRC IGATTLDEYR KYIEKDAALE RRFQPVYIGE PSVEDTVAIL RGLKERYDLH
HGVRIKDSAL VAAATLSHRY ISERFLPDKA IDLIDEAASK LRMEIDSMPT ELDEVERKIT
QLEIEKKSLK KETDEESKKR VEKLERQLSG LKEDGSALRL HWENEKKVIK EIQDLNAKID
QAKVDEQTAQ RNGDLEKVAE IRYSLLRDYD NDIQKLHERL KDIQKDRCLL KEEVDTDDIA
EVVSKWTGIP VSRMLESEKE KLIRMEERLK ERVVGQGDAI EAVSNAVRRA RAGLQDPDRP
IGTFLFLGPT GVGKTELCKA LASFLFDDES AMVRIDMSEF MEQHSVARLI GAPPGYVGYE
EGGRLTEAIR RRPYSVILFD EIEKAHKDIF NILLQVFDDG RLTDGHGRTV DFRNVIIVMT
SNIGSQYIQD FIAHGNREEL DKNISKTLKE IFRPEFLNRI DETIIFSSLT KEQIGDIVEI
QLAELKKRLS QHNLKLSVTE SAKKCLVEEG YDVFYGARPL KRTIQQRIEN PLSLEILQRK
FEKADEIIVD SEGGSLTFQT KGR
//
