ID A0A2M9E8Q6_9GAMM Unreviewed; 869 AA.
AC A0A2M9E8Q6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=CO641_00605 {ECO:0000313|EMBL:PJK00524.1};
OS Xanthomonadaceae bacterium NML91-0213.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae.
OX NCBI_TaxID=2032582 {ECO:0000313|EMBL:PJK00524.1, ECO:0000313|Proteomes:UP000229012};
RN [1] {ECO:0000313|EMBL:PJK00524.1, ECO:0000313|Proteomes:UP000229012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML91-0213 {ECO:0000313|EMBL:PJK00524.1,
RC ECO:0000313|Proteomes:UP000229012};
RA Bernier A.-M., Bernard K.;
RT "Zoonotically transmitted species of Xanthomonadaceae : Genome sequencing
RT and assembly.";
RL Submitted (SEP-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 -!- 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:PJK00524.1}.
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DR EMBL; NWQL01000001; PJK00524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9E8Q6; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000229012; 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 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 869 AA; 95548 MW; C6D0969BEB36DD51 CRC64;
MRMDKLTSRF QQAIADAQSL AVGRDHNLIE PVHLLVALID QQGGGTRPLL SQAGVNVPLL
RERLGEVLEG LPRVSGQAGQ VSVGNDLARL LNHTDKLAQQ RGDAYIASEL FLLAAMEDGG
DAGRALKAAG ADRARLEAAI DAMRGGEAVA DENAEDARQA LQKYTIDLTA RAESGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNNEVPE GLRGKRVLSL
DMGALIAGAK FRGEFEERLK AVLNDLAKNE GQIILFIDEL HTMVGAGKAE GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVFVGE PSVEDTIAIL RGLKEKYAVH
HGVEITDPAI VAAATLSNRY IADRQLPDKA IDLMDEAASR IRMEIDSKPE ELDRRERRLI
QLKIQREALK KEKDDASRQR LADLEAEIAK LEREYNDLEE VWKAEKATVQ GATKIKEQIE
AARLELEAAQ RRQDFAKMSE IQYGRLPELE KQLKAAQEAE TTGFTLLQDK VTAEEIAEVV
ARWTGIPVNR MLEGEREKLL RMEEMLHARV VGQDEAIRVV SDAVRRSRAG LSDPDRPSGS
FLFLGPTGVG KTELSKALAE FLFDSAEAMV RIDMSEFMEK HAVSRLVGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIIMTSNL
GSQMIQELAG EGGAGGDEGQ SAIAYTQMKA AVMGVVQAHF RPEFINRLDD IVVFHPLQKA
QIRQIARIQL RGLEQRLAER GLKLEISEAA FDLLGNVGFD PVYGARPLKR AVQQALENPL
AQKILAGEFS AGDTIRVDAE AGALVFAKG
//