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Database: UniProt
Entry: A0A498DT97_9PROT
LinkDB: A0A498DT97_9PROT
Original site: A0A498DT97_9PROT 
ID   A0A498DT97_9PROT        Unreviewed;       864 AA.
AC   A0A498DT97;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RLL53724.1};
GN   ORFNames=D8Y20_04695 {ECO:0000313|EMBL:RLL53724.1};
OS   Mariprofundus sp. EBB-1.
OC   Bacteria; Pseudomonadota; Zetaproteobacteria; Mariprofundales;
OC   Mariprofundaceae; Mariprofundus.
OX   NCBI_TaxID=2650971 {ECO:0000313|EMBL:RLL53724.1, ECO:0000313|Proteomes:UP000270267};
RN   [1] {ECO:0000313|Proteomes:UP000270267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EBB-1 {ECO:0000313|Proteomes:UP000270267};
RA   Lopez A., Barco R., Canela R., Emerson D., Tully B., Abuyen K.,
RA   Broomell S., Albino D., Beraki S., Dingmon T., Estrada S., Fernandez M.,
RA   Amend J.;
RT   "Genome Sequence of Zetaproteobacterium sp. EBB-1: a novel, marine, iron-
RT   oxidizing chemolithoautotroph isolated from an iron-sulfide mineral.";
RL   Submitted (OCT-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:RLL53724.1}.
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DR   EMBL; RCFQ01000007; RLL53724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498DT97; -.
DR   Proteomes; UP000270267; 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   Reference proteome {ECO:0000313|Proteomes:UP000270267};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..151
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          417..497
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   864 AA;  96061 MW;  754280A25DC6303C CRC64;
     MDLSRMTQKL NEAMAASQSL AARLSHQQVD GEHLLAELLA QDDGLAPRLI ERAGRDINVF
     KSDIQSALSR HPKVSGQRVE IDKIYITQRL QGLLAKAAAE AERMQDDYIS VEHVLLTFID
     EKDSSEAGKI FKAQGITRES FLEVLGSVRG NQRVTTDAPE SQYEALKKYG VDLVELARSG
     KLDPVIGRDA EIRSVIRILS RKTKNNPVLI GEPGVGKTAI AEGLAQRIVS GDVPEGLKNR
     SLFSLDMTSL MAGAKYRGEF EERLKAVLEE IKASEGHTLL FIDELHTIVG AGKTEGSSDA
     GNMLKPMLAR GELHCIGATT LNEYRLYIEK DAALERRFQP VMVDAPDVAD TISILRGIRE
     RFELHHGVRI SDAALVAAAT LSDRYISDRF LPDKAIDLVD EACASIRTEM DSMPAELDAI
     SRRAMRLEIE ETALKKEKDE ASRKRLNILR KELVELQEQR DVMRARWEQE KGAMGNVQSL
     REQIEQVKLD IESAERRYDL EITASLRYGT LPALEKQLAE QEASVQAREG LISEVVNEAE
     IAAVVARWTG IQMTRLLQGE REKLLSLESV LHERVIGQDE AVLAVSNAVL RARAGIRDQH
     KPIGSFLFLG PTGVGKTELA RTLARTLFDA EENMVRIDMS EYMEKHAVSR LLGAPPGYIG
     FEQGGQLTEA VRRKPYCVLL LDEVEKAHPD VFNVLLQLLD DGRLTDSHGR TVNFQHTIVI
     MTSNIGSEYM LDGIDADGAL NETASAQIMA ALTQHFRPEF LNRVDETVLF RPLTQNVVAR
     IVEVFLMELK QRLSEQQVSL TVTDEAVQWI AVQAYDPAFG ARPLKRFIQE HLETPLARLL
     IADEAGTNVV VDVVDNGLSV HGDK
//
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