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Database: UniProt
Entry: A0A0Q9EMA4_9GAMM
LinkDB: A0A0Q9EMA4_9GAMM
Original site: A0A0Q9EMA4_9GAMM 
ID   A0A0Q9EMA4_9GAMM        Unreviewed;       861 AA.
AC   A0A0Q9EMA4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=ASE45_14685 {ECO:0000313|EMBL:KRD67957.1};
OS   Lysobacter sp. Root96.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD67957.1, ECO:0000313|Proteomes:UP000050805};
RN   [1] {ECO:0000313|EMBL:KRD67957.1, ECO:0000313|Proteomes:UP000050805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root96 {ECO:0000313|EMBL:KRD67957.1,
RC   ECO:0000313|Proteomes:UP000050805};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD67957.1, ECO:0000313|Proteomes:UP000050805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root96 {ECO:0000313|EMBL:KRD67957.1,
RC   ECO:0000313|Proteomes:UP000050805};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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. {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:KRD67957.1}.
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DR   EMBL; LMJN01000003; KRD67957.1; -; Genomic_DNA.
DR   RefSeq; WP_055900367.1; NZ_LMJN01000003.1.
DR   AlphaFoldDB; A0A0Q9EMA4; -.
DR   STRING; 1736612.ASE45_14685; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000050805; 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:UP000050805};
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   861 AA;  94955 MW;  3EE517BA25E1542E CRC64;
     MRMDKLTSRF QQALADAQSL AVGRDHSVIE PAHLLSALLD QSGGSTRPLL AQAGVNVPLL
     RERLGETLEK LPKVSGQAGN VSLGNDLARL LNVTDKLAQQ RGDAFIASEL FLLAALEDGG
     DVGRALKAAG ASKAKLEPAI DKLRGGESVQ SENAEEQRQA LEKYCIDLTA RAESGKLDPV
     VGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINNEVPE GLRGKRVLSL
     DMGALIAGAK FRGEFEERLK AVLSDLSKNE GQVILFIDEL HTMVGAGKAE GSMDAGNMLK
     PALARGELHC IGATTLDEYR KYVEKDAALE RRFQKVFVGE PSVEDTIAIL RGLKERYAVH
     HGVEITDPAI VAAATLSHRY IADRQLPDKA IDLMDEAASR IRMEIDSKPE ELDRKERRLI
     QLKIQREALK KEKDAESKQR LADLEAEIAT LERDFNDLEE IWKAEKATLQ GATKIKEQIE
     QAKLELEAAQ RTQDYARMSE IQYGALPELE KQLKAAQEAE TQGFRLLQDK VTAEEIAEVV
     ARWTGIPVSK MLEGEREKLL KMEQALHQRV VGQDEAIRVV SDAVRRSRAG LSDPDRPSGS
     FLFLGPTGVG KTELCKALAE FLFDSSDAMV RIDMSEFMEK HAVSRLVGAP PGYVGYEEGG
     YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
     GSQMIQELAS DDSAESYTQM KAAVMGVVQA HFRPEFINRL DDIVVFHPLD KVQIREIAKI
     QMHGLEKRLG ERGLKLSLSD AALALIGNVG FDPVYGARPL KRAVQQQLEN PLAQKILSGE
     FVSGDTIQVE AEAGHLVFRK A
//
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