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Database: UniProt
Entry: C6XG47_LIBAP
LinkDB: C6XG47_LIBAP
Original site: C6XG47_LIBAP 
ID   C6XG47_LIBAP            Unreviewed;       853 AA.
AC   C6XG47;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 95.
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:ACT57350.1};
GN   OrderedLocusNames=CLIBASIA_03870 {ECO:0000313|EMBL:ACT57350.1};
OS   Liberibacter asiaticus (strain psy62).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=537021 {ECO:0000313|EMBL:ACT57350.1, ECO:0000313|Proteomes:UP000002744};
RN   [1] {ECO:0000313|EMBL:ACT57350.1, ECO:0000313|Proteomes:UP000002744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX   PubMed=19589076; DOI=10.1094/MPMI-22-8-1011;
RA   Duan Y., Zhou L., Hall D.G., Li W., Doddapaneni H., Lin H., Liu L.,
RA   Vahling C.M., Gabriel D.W., Williams K.P., Dickerman A., Sun Y.,
RA   Gottwald T.;
RT   "Complete genome sequence of citrus huanglongbing bacterium, 'Candidatus
RT   Liberibacter asiaticus' obtained through metagenomics.";
RL   Mol. Plant Microbe Interact. 22:1011-1020(2009).
RN   [2] {ECO:0000313|EMBL:ACT57350.1, ECO:0000313|Proteomes:UP000002744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX   PubMed=21784907; DOI=10.1128/AEM.05111-11;
RA   Zhou L., Powell C.A., Hoffman M.T., Li W., Fan G., Liu B., Lin H., Duan Y.;
RT   "Diversity and plasticity of the intracellular plant pathogen and insect
RT   symbiont, 'Candidatus Liberibacter asiaticus', revealed by hyper variable
RT   prophage genes with intragenic tandem repeats.";
RL   Appl. Environ. Microbiol. 77:6663-6673(2011).
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. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK.
CC       {ECO:0000256|ARBA:ARBA00025613}.
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|ARBA:ARBA00004496,
CC       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; CP001677; ACT57350.1; -; Genomic_DNA.
DR   RefSeq; WP_015452710.1; NC_012985.3.
DR   AlphaFoldDB; C6XG47; -.
DR   STRING; 537021.CLIBASIA_03870; -.
DR   GeneID; 66286345; -.
DR   KEGG; las:CLIBASIA_03870; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_5; -.
DR   OMA; ERMKAVM; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000002744; 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: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 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   Hydrolase {ECO:0000313|EMBL:ACT57350.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ACT57350.1};
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..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   853 AA;  95765 MW;  45BDDC14C20B26E3 CRC64;
     MNSDKYSDLM RNVLQSAQTY ALAQGHQNLV PEHVLHIFLE DEQGAVYSLI QCSGGDIAQL
     KDYNQTVLSK IPKVTGGGAQ VYLSQPLAVI LSKSEEIAKK SGDSFVTAEK FLLAMVMETG
     GIGESLKKCG LKFSRLEESI KKLRKGRVAD SVNAEQGFDA LKKYCRDLTE EARNGKLDPV
     IGRDDEMRRA IQVLSRRTKN NPVLIGDPGV GKTAIIEGLA SRIINGDIPE SLKGKRLMAL
     DMGALIAGAK FRGEFEERLK SLLCEIRSED GEIILFIDEL HVLVGAGKTD GAMDASNLLK
     PSLARGELHC IGATTLDEYR KYIEKDPALA RRFQSLLVGE PTVTDTISIL RGLKERYEQH
     HKVRISDSAL VSAAVLSNRY ITDRFLPDKA IDLMDEASAR VRMQIDTKPE VLDELDRRII
     CLKIEKEALK KEKDSFSKGR LIELEKELSS LEEKSHSLTL RWQEGQRKIL YVADLKKRLE
     SMRNELAIAQ RQGHFERAGE LAYGLIPKTE KELDEAEKAD STAEDMVQEV VTSDNIANIV
     SRWTGIPVDK MLESDREKFL RIETEISKSV IGQSAAVESV SNALRRFRAG LQDPQRPMGS
     FMFLGPTGVG KTELVKSLAR LLFDDENSMI RIDMSEYMEK HSVSRLIGSP PGYVGYEEGG
     ALTEAVRRHP YQVVLFDEIE KAHSDVHNIL LQVLDDGRLT DSQGRTVDFR NTLIIMTSNL
     GAEYLIEDGD SVHDKVMGIV RSAFKPEFLN RLDEIILFEK LRKEDMAKIV RIQLGRVLSL
     IKERNISMDF DDQVIDWLSC RGYDPSYGAR PLKRVIQRYI QNPLAERVLS QTISDGDSIE
     VFVDDDNLNF RVI
//
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