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Database: UniProt
Entry: A0A1I4ACV7_9ACTN
LinkDB: A0A1I4ACV7_9ACTN
Original site: A0A1I4ACV7_9ACTN 
ID   A0A1I4ACV7_9ACTN        Unreviewed;       883 AA.
AC   A0A1I4ACV7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SAMN04488085_102154 {ECO:0000313|EMBL:SFK53636.1};
OS   Geodermatophilus ruber.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=504800 {ECO:0000313|EMBL:SFK53636.1, ECO:0000313|Proteomes:UP000199152};
RN   [1] {ECO:0000313|EMBL:SFK53636.1, ECO:0000313|Proteomes:UP000199152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45317 {ECO:0000313|EMBL:SFK53636.1,
RC   ECO:0000313|Proteomes:UP000199152};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOSW01000002; SFK53636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4ACV7; -.
DR   STRING; 504800.SAMN04488085_102154; -.
DR   InParanoid; A0A1I4ACV7; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000199152; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   Hydrolase {ECO:0000313|EMBL:SFK53636.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SFK53636.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199152};
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..538
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   883 AA;  98179 MW;  C17785760EB8D076 CRC64;
     MDLNRLTQKS QEALAAAQAL AIQHGHTEVD VEHLLLALLD QSEGLVPRLL AAMDVDLAAL
     RRDVEAEVSR KPRTTGAAPQ PGQVSLTQRV ARVLETADRE ARRMKDEYVS VEHLLVALVE
     TGQTTGAGRV LAQHGVTRDA FLSALTQIRG NQRVTSATPE GTYEALAKYG MDLVEAARTG
     RMDPVIGRDA EIRRVIQILS RKSKNNPVLL GEPGVGKTAI VEGLAQRIVN GDVPEGLRDR
     TIFALDMGLL VAGAKYRGEF EERLQAVLTE VKAAEGRVLL FIDEVHNVVG AGASEGAMDA
     GNMLKPMLAR GELHMIGATT LTEYRKYIEK DAALERRFQP VFVEEPSVED TISILRGLRE
     RFEVFHGVRI LDGALVAAAT LSHRYLTDRF LPDKAIDLVD EACARLRTEI DSMPAELDEI
     TRRVMRLEIE EAALEKEDDP ASIARLDQLR RELADLRAEA DAMRAQWNAE RQAIQRVQEL
     RAELEQVRRE IEEAERSYDL NRAAELRYGR LAELERKLEA EEQRLAAKQG ENRLLREVVT
     PEEIAEIVSS WTGIPVSRLT EGEREKLLRL DELLHQRVIG QEEAVQAVAD AIIRARSGVK
     DPRRPTGSFI FLGPTGVGKT ELAKALAEAL FDSEENIVRI DMSEYQERHT VSRLVGAPPG
     YVGYEEGGQL TEAVRRRPYA VVLFDEIEKA HPDVFNTLLQ VLDDGRLTDA QGRTVDFRNT
     VIIMTSNIGS QYLLDGVTAD GQLKPEARDL VLAELRSHFR PEFLNRVDDT VLFKPLTPAQ
     IEHIVELMLA DLRKRLAERN ITLEVTDEAR RFIAREGYDP VYGARPLRRF IAKEVETRVA
     RALLRAGALE GETIRVDVEG GHLVVAVQAP TGAQADQQAG AQV
//
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