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Database: UniProt
Entry: A0A132PHV4_9MYCO
LinkDB: A0A132PHV4_9MYCO
Original site: A0A132PHV4_9MYCO 
ID   A0A132PHV4_9MYCO        Unreviewed;       848 AA.
AC   A0A132PHV4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=AFM11_23605 {ECO:0000313|EMBL:KWX21834.1};
OS   Mycolicibacterium wolinskyi.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX21834.1, ECO:0000313|Proteomes:UP000070612};
RN   [1] {ECO:0000313|EMBL:KWX21834.1, ECO:0000313|Proteomes:UP000070612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC_01 {ECO:0000313|EMBL:KWX21834.1,
RC   ECO:0000313|Proteomes:UP000070612};
RA   de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA   Limbago B.M., Noble-Wang J.;
RT   "A draft genome sequence of Mycobacterium wolinskyi.";
RL   Submitted (JUL-2015) 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. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
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:KWX21834.1}.
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DR   EMBL; LGTW01000017; KWX21834.1; -; Genomic_DNA.
DR   RefSeq; WP_067853275.1; NZ_LGTW01000017.1.
DR   AlphaFoldDB; A0A132PHV4; -.
DR   STRING; 59750.AWC31_28330; -.
DR   PATRIC; fig|59750.3.peg.2077; -.
DR   Proteomes; UP000070612; 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:UP000070612};
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   848 AA;  92459 MW;  940B583D0186B4E2 CRC64;
     MDSFNPTTKT QAALTSALQA ATAAGNPQIT PAHLLMALLT QNDGIAAPLL EAVGVEPATI
     RTEAERLIGR LPSATGSSSQ PQLSPEAITA ITTAQHLATE MDDEYVSTEH LMVGLATGSS
     EVAKLLTNNG ASPQALREAF TKVRGSARVT SPDPEGSYQA LEKYSTDLTA RAREGKLDPV
     IGRDNEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRDKTVISL
     DLGSMVAGAK YRGEFEERLK AVLDDIKNSA GQVITFIDEL HTIVGAGATG ESAMDAGNMI
     KPMLARGELR LVGATTLDEY RKYIEKDAAL ERRFQQVLVG EPSVEDTVGI LRGLKDRYEV
     HHGVRITDSA LVAAATLSDR YITARFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEVERLV
     RRLEIEEMAL EKESDEASKD RLEKLRAELA DHKEKLAELT TRWQNEKGAI DVVRELKEQL
     DTLRGEADRA ERDGDLAKAA ELRYGRIPEV EKKLDAALPV AEARENVMLK EEVGPDDIAE
     VVEAWTGIPA GRMLEGETAK LLRMEEELGK RVVGQKKAVV AVSDAVRRSR AGVADPNRPT
     GSFMFLGPTG VGKTELAKAL AEFLFDDERA MVRIDMSEYG EKHSVARLVG APPGYIGYDQ
     GGQLTEAVRR RPYTVVLFDE IEKAHPDVFD VLLQVLDEGR LTDGQGRTVD FRNTILILTS
     NLGAGGTEEH VMAAVRAAFK PEFINRLDDV IIFDGLNPEE LVSIVDIQLG QLAKRLAQRR
     LTLEVSLPAK KWLAERGFDP LYGARPLRRL VQQAIGDQLA KMLLAGEVHD GDIVPVNLSP
     DGESLVLG
//
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