ID A0A1N6NFF1_9GAMM Unreviewed; 860 AA.
AC A0A1N6NFF1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=SAMN05421546_0241 {ECO:0000313|EMBL:SIP90820.1};
OS Lysobacter tolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1604334 {ECO:0000313|EMBL:SIP90820.1, ECO:0000313|Proteomes:UP000241788};
RN [1] {ECO:0000313|EMBL:SIP90820.1, ECO:0000313|Proteomes:UP000241788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UM1 {ECO:0000313|EMBL:SIP90820.1,
RC ECO:0000313|Proteomes:UP000241788};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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 ---------------------------------------------------------------------------
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; FTLW01000001; SIP90820.1; -; Genomic_DNA.
DR RefSeq; WP_076584649.1; NZ_FTLW01000001.1.
DR AlphaFoldDB; A0A1N6NFF1; -.
DR STRING; 1604334.SAMN05421546_0241; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000241788; 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 78, MITOCHONDRIAL; 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:SIP90820.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SIP90820.1};
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..499
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 860 AA; 95372 MW; E392D2EDA4B7F6EA CRC64;
MRMDKLTSRF QQAIADAQSL AVGRDNSIIE PAHLLLALLD QQGGGTKPLL AQAGVNVPVL
WERLTEALDR LPKVSGQAGN VSVSNDLSRL LNVTDKLAQQ RGDAFIASEL FLLAALEDGG
DAGRALKVAG ANKAQLETAI DNMRGGDTVQ DENAEDQRQA LEKYTVDLTA RHEKGKLDPV
IGRDEEIRRC IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNNEVPE GLRGKRVLSL
DMGALIAGAK FRGEFEERLK AVLNDLSKSE GQIILFIDEL HTMVGAGKAD GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVFVGE PSVEDTIAIL RGLKEKYAVH
HGVEITDPAI VAAATLSNRY ITDRQLPDKA IDLMDEAASR IRMEIDSKPE ELDRKERRLI
QLKIQREALK KEKDDASKQR LADLEEEIKG LERDYNDLEE VWKSEKATLQ GATKIKEQIE
DARLQLEAAQ RQQDFARMSE IQYGTLPELE KQLKAAQEVE TTGFRLLQDK VTAEEIAEVV
SRWTGIPVSK MLEGEREKLL KMEEHLHTRV VGQEEAIKVV SDAVRRSRAG LSDPNRPSGS
FLFLGPTGVG KTELTKALAD FLFDSPDAMI RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
GSHQIQELAG DDSPEAYVQM KAAVMGVVQA HFRPEFINRL DDIVVFHPLD KQQIKQIAKI
QLGGLEKRLA ERGIKLELSD KAYELLGNVG FDPVYGARPL KRAIQQQIEN PLAQQILSGQ
FTNGDTVKVD AEGGKLVFQR
//
