ID M4TXB2_9XANT Unreviewed; 861 AA.
AC M4TXB2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=XAC29_16255 {ECO:0000313|EMBL:AGH78674.1};
OS Xanthomonas axonopodis Xac29-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1304892 {ECO:0000313|EMBL:AGH78674.1, ECO:0000313|Proteomes:UP000011979};
RN [1] {ECO:0000313|EMBL:AGH78674.1, ECO:0000313|Proteomes:UP000011979}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xac29-1 {ECO:0000313|EMBL:AGH78674.1,
RC ECO:0000313|Proteomes:UP000011979};
RA Chen G., Zou H., Ye G., Song X., Ji Z., Ma W.;
RT "Completed genome of Xanthomonas axonopodis sp. Xac29-1.";
RL Submitted (MAR-2013) 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; CP004399; AGH78674.1; -; Genomic_DNA.
DR RefSeq; WP_015463505.1; NC_020800.1.
DR AlphaFoldDB; M4TXB2; -.
DR SMR; M4TXB2; -.
DR GeneID; 66912259; -.
DR KEGG; xao:XAC29_16255; -.
DR PATRIC; fig|1304892.4.peg.3400; -.
DR HOGENOM; CLU_005070_4_2_6; -.
DR Proteomes; UP000011979; 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 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:AGH78674.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:AGH78674.1};
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 405..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 861 AA; 95575 MW; D389BD4A69583301 CRC64;
MRMDKLTSRF QQALADAQSL AVGRDHNIIE PVHVLAALLD QSGGSTRPLL SQAGVNVPLL
RERLGEALDT LPKVSGQEGN LSIGNDLNRL LNQTDKLAQQ HGDAFIASEW FVLAAADDAS
PLGVALRAAG GDKKKIEAAI DKLRGGETVQ SENAEEQRQA LEKYTIDLTA RAESGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLRGKRVLSL
DMGALIAGAK FRGEFEERLK AVLSDLSKNE GQIILFIDEL HTMVGAGKAD GAMDAGNMLK
PALARGELHC IGATTLDEYR KYIEKDAALE RRFQKVFVGE PTVEDTIAIL RGLKERYAVH
HGVEITDPAI VAAATLSNRY ITDRQLPDKA IDLMDEAASR IRMEIDSKPE ELDRLERRLI
QLKIQREMLK KEKDDASRQR LADLETDIDK LEREFYDLNE LWKSEKAALQ GTTKVKEQIE
HAKLELEAAQ RRQDYAKMSE IQYGVLPQLE KQMALANEVE HHDFKLVQDR VTAEEIAEVV
SRWTGIPVNK MLEGERDKLL RMEDELHHRV VGQNEAIKVV SDAVRRSRAG LSDPNRPSGS
FLFLGPTGVG KTELCKALAD FLFDSTEAMI RIDMSEFMEK HSVARLIGAP PGYVGYEEGG
YLTEAVRRRP YSLILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVIVMTSNL
GSHQIQELSG DDSAEAYTQM KAAVMGVVQA HFRPEFINRL DDIVVFHPLD KAQIKSIARI
QLQGLEKRLA ERGLKLDLDD AALEVLGSVG FDPVYGARPL KRAIQSQVEN PLAQQILSGQ
YLSGDSVRVR ADGGRLVFTK D
//
