GenomeNet

Database: UniProt
Entry: A0A014M2D9_9GAMM
LinkDB: A0A014M2D9_9GAMM
Original site: A0A014M2D9_9GAMM 
ID   A0A014M2D9_9GAMM        Unreviewed;       857 AA.
AC   A0A014M2D9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=BG55_07755 {ECO:0000313|EMBL:EXU76026.1};
OS   Erwinia mallotivora.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU76026.1, ECO:0000313|Proteomes:UP000019918};
RN   [1] {ECO:0000313|EMBL:EXU76026.1, ECO:0000313|Proteomes:UP000019918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU76026.1,
RC   ECO:0000313|Proteomes:UP000019918};
RA   Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA   Mat Amin N.;
RT   "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT   pathogen.";
RL   Submitted (FEB-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:EXU76026.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JFHN01000039; EXU76026.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A014M2D9; -.
DR   STRING; 69222.BG55_07755; -.
DR   PATRIC; fig|69222.5.peg.1596; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000019918; 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:UP000019918};
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          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   857 AA;  94961 MW;  40FC1C5352305B73 CRC64;
     MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLS QDGGSVRPLL TTAGVDVASL
     NSSVQQAISR LPQVEGSDGD VQPSADLVRV LNLCDKLAQK RADNFISSEL FVLAALDSRG
     SLADLLKSAG ATSENLTRAV EQMRGGENVN DQGAEDQRQA LKKYTIDLTE RAEMGKLDPV
     IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL
     DMGALVAGAK YRGEFEERLK GVLNDLSKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK
     PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PGVEDTIAIL RGLKERYELH
     HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRMQIDSKPE SLDRLERRII
     QLKLEQQALK KESDEASIKR LDMLESELTQ KERDYSELEE EWKAEKASLS GTQTIKAELE
     QAKLSLEQAR RSGDLAQMSE LQYGKIPELE KQLALATQSE GKTMRLLRNR VTDIEIADVL
     ARWTGIPVAR MMEGERDKLL RMEQELHKRV IGQDEAVTAV SNAIRRSRAG LADPNRPVGS
     FLLLGPTGVG KTELCKALAN FLFDSDDAMV RLDMSEFMEK HAVSRLVGAP PGYVGYEEGG
     YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
     GSDLIQERFG ALSYAEMKDV VMAVVGQHFR PEFINRIDEL VVFHPLGEKH IASIAKIQLQ
     RLYDRLAERG YTLHISDEAL QMLGENGYDP VYGARPLKRA IQQQIENPLA QQILSGSLTP
     GKLIEMDVQN GAIVAHQ
//
DBGET integrated database retrieval system