ID A0A0S2DLP9_LYSEN Unreviewed; 861 AA.
AC A0A0S2DLP9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:ALN59440.1};
GN ORFNames=FE772_20100 {ECO:0000313|EMBL:QCW27597.1}, GLE_4098
GN {ECO:0000313|EMBL:ALN59440.1};
OS Lysobacter enzymogenes.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=69 {ECO:0000313|EMBL:ALN59440.1, ECO:0000313|Proteomes:UP000061569};
RN [1] {ECO:0000313|EMBL:ALN59440.1, ECO:0000313|Proteomes:UP000061569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3 {ECO:0000313|EMBL:ALN59440.1,
RC ECO:0000313|Proteomes:UP000061569};
RA Kobayashi D.Y.;
RT "Genome sequences of Lysobacter enzymogenes strain C3 and Lysobacter
RT antibioticus ATCC 29479.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QCW27597.1, ECO:0000313|Proteomes:UP000308311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC36 {ECO:0000313|EMBL:QCW27597.1,
RC ECO:0000313|Proteomes:UP000308311};
RA Feng T.;
RT "Intraspecies Signal LeDSF and Interspecies Signal Indole Synergistically
RT Regulate the Twitching Motility of Lysobacter enzymogenes.";
RL Submitted (MAY-2019) 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; CP013140; ALN59440.1; -; Genomic_DNA.
DR EMBL; CP040656; QCW27597.1; -; Genomic_DNA.
DR RefSeq; WP_057948780.1; NZ_CP040656.1.
DR AlphaFoldDB; A0A0S2DLP9; -.
DR STRING; 69.GLE_4098; -.
DR KEGG; lez:GLE_4098; -.
DR PATRIC; fig|69.6.peg.4040; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000061569; Chromosome.
DR Proteomes; UP000308311; Chromosome.
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:UP000061569};
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; 94901 MW; 6B9701E0C19727A4 CRC64;
MRMDKLTSRF QQALQDAQSL AVGRDHSVIE PAHLLTALLD QSGGSTRPLL AQSGVNVPLL
RERLGEALEK LPKVSGQAGN VSLGNDLARL LNVTDKLAQQ RNDAFIASEL FLLAALDDGG
DAGRALKAAG ATKAKLEPAI DKLRGGESVQ SESAEDQRQA LEKYCIDLTA RAENGKLDPV
VGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNNEVPE GLRGKRVLSL
DMGALIAGAK FRGEFEERLK AVLNDLSKNE GQVILFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC IGATTLDEYR KYVEKDAALE RRFQKVFVGE PTVEDTIAIL RGLKERYAVH
HGVEITDPAI VAAATLSHRY IADRQLPDKA IDLMDEAASR IRMEIDSKPE ELDRKERRLI
QLKIQREALK KEKDAESKQR LADLEAEIAT LERDFNDLEE VWKAEKATLQ GATKIKEQIE
QAKLDLEAAQ RTQDFGRMSE IQYGKLPELE KQLKAAQEAE TQGFKLLQDK VTAEEIAEVV
ARWTGIPVAK MLEGERDKLL KMEQALHARV VGQDEAVRVV SDAVRRSRAG LSDPNRPSGS
FLFLGPTGVG KTELCKALAE FLFDSSDAMI RIDMSEFMEK HAVSRLVGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
GSQMIQELSN DNTPEAYTQM KAAVMGVVQT HFRPEFINRL DDIVVFHPLE KSQIREIAKI
QLHGLEKRLA ERGLKLSLSE AALTLIGNVG FDPVYGARPL KRAVQQQIEN PLAQKILSGE
FVNGDTIQVD AAGGHLVFAK G
//