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Database: UniProt
Entry: A0A372J7I6_9ACTN
LinkDB: A0A372J7I6_9ACTN
Original site: A0A372J7I6_9ACTN 
ID   A0A372J7I6_9ACTN        Unreviewed;       861 AA.
AC   A0A372J7I6;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RFU23162.1};
GN   ORFNames=D0Z06_00435 {ECO:0000313|EMBL:RFU23162.1};
OS   Geodermatophilus sp. LHW52908.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=2303986 {ECO:0000313|EMBL:RFU23162.1, ECO:0000313|Proteomes:UP000262362};
RN   [1] {ECO:0000313|EMBL:RFU23162.1, ECO:0000313|Proteomes:UP000262362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW52908 {ECO:0000313|EMBL:RFU23162.1,
RC   ECO:0000313|Proteomes:UP000262362};
RA   Li L., Lin H.W.;
RT   "Geodermatophilus marinus sp. nov., isolated from marine sponge Leucetta
RT   chagosensis.";
RL   Submitted (AUG-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:RFU23162.1}.
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DR   EMBL; QVQH01000001; RFU23162.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372J7I6; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000262362; 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:UP000262362};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..493
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   861 AA;  93474 MW;  7EE55134255F13BA CRC64;
     MQSKLTTRSQ EAIAAAQRLA VDRGQAALEP LHLLVALLEQ TDGIAGPLLR AVGTDASDVR
     AKAEAAVRRM PSVSGATVPA PAPSREFLRV LNAAGEQASA LGDEFVSTEH LLVGLADAGG
     EAGAVLSSAG ATRDALLAAF RTVRGSRKVT TPDPEGTFQA LQKYAVDLTE RAREGRIDPV
     VGRDTEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLKGKRLMAL
     DLASMVAGAK YRGEFEERLK AVLQEITDAE GEVITFIDEL HTIVGAGATG EGAMDAGNMI
     KPMLARGELR MVGATTLDEY REHIEKDPAL ERRFQQVLVG EPSVEDTIGI LRGLKERYEV
     HHGVRITDAA IVAAAALSDR YVTARFLPDK AIDLVDEAAS RLRMEIDSRP VEVDEVERAV
     RRLEIEEMAL AKEDDPSSVE RLGALRADLA DKRQQLDELT ARWQQDKGAI VRIQQIKEEL
     ERLRTEAERA ERDGELAHVA ELRYGRIPQL EKALTEAEAS VEDGGSMLKE EVGPDDIADV
     VQAWTGIPAG RLLEGETQKL LRMEDELGAR VVGQPDAVRA VSDAVRRARS GVADPDRPTG
     SFLFLGPTGV GKTELAKALA EFLFDDERAM VRIDMSEYSE KHSVARLVGA PPGYVGYEAG
     GQLTEAVRRR PYTVVLLDEV EKAHPDVFDV LLQVLDDGRL TDGQGRTVDL RNTILILTSN
     LGSQLIADQS VEEERRRAAV LEVVRSHFKP EFLNRLDDVV VFRALGSEEL AGIVDIQVGV
     LARRLAARRL TLDVTDAARE WLALNGFDPV YGARPLRRLV QSAIGDQLAK ALLAGDIRDG
     DRVLVDAPED LSVDGLTVTR G
//
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