ID I0RHI5_MYCXE Unreviewed; 848 AA.
AC I0RHI5;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=MXEN_17777 {ECO:0000313|EMBL:EID10588.1};
OS Mycobacterium xenopi RIVM700367.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1150591 {ECO:0000313|EMBL:EID10588.1, ECO:0000313|Proteomes:UP000003584};
RN [1] {ECO:0000313|EMBL:EID10588.1, ECO:0000313|Proteomes:UP000003584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIVM700367 {ECO:0000313|EMBL:EID10588.1,
RC ECO:0000313|Proteomes:UP000003584};
RX PubMed=22628510; DOI=10.1128/JB.00482-12;
RA Abdallah A.M., Rashid M., Adroub S.A., Elabdalaoui H., Ali S.,
RA van Soolingen D., Bitter W., Pain A.;
RT "Complete Genome Sequence of Mycobacterium xenopi Type Strain RIVM700367.";
RL J. Bacteriol. 194:3282-3283(2012).
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|ARBA:ARBA00004496,
CC 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:EID10588.1}.
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DR EMBL; AJFI01000088; EID10588.1; -; Genomic_DNA.
DR RefSeq; WP_003922462.1; NZ_AJFI01000088.1.
DR AlphaFoldDB; I0RHI5; -.
DR PATRIC; fig|1150591.3.peg.3585; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000003584; 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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000003584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 1..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 413..500
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 848 AA; 92997 MW; FB3B470B4C56098A CRC64;
MDSFNPTTKT QAALTSALQA ASAAGHPEIR PAHLLMALLT QNDGIAAPLL EAVGVEPATI
RAEAQRLIDR LPQVTGASSQ PQLSRESLAA ITAAQQLATE MDDEYVSTEH LMVGLATGDS
DVAKLLNGHG ASPQALREAF VKVRGSARVT SPDPEATYQA LEKYSTNLTA AAREGKLDPV
IGRDTEIRRV VQVLSRRTKN NPVLIGEPGV GKTAIVEGLA QRIVAGDVPE SLRDKTIIAL
DLGSMVAGSK YRGEFEERLK AVLEDIKNSA GQIITFIDEL HTIVGAGATG EGSMDAGNMI
KPMLARGELR LVGATTLDEY RKHIEKDAAL ERRFQPVYVG EPSVEDTIGI LRGLKDRYEV
HHGVRITDSA LVAAATLSDR YITARFLPDK AIDLVDEAAS RLRMEIDSRP VEIDEVERLV
RRLEIEEMAL AKEEDEASRE RLEKLRAELA DQKEKLAELT TRWQNEKNAI DTVRELKEQL
ERLRGESERA ERDGDLAKAA ELRYGRIPEV EKKLEAALPQ AQAREAMMLK EEVGPDDIAE
VVSAWTGIPA GRLLEGETAK LLRMEDELSK RVVGQRRAVQ AVSDAVRRSR AGISDPNRPT
GAFMFLGPTG VGKTELAKAL AEFLFDDERA MVRIDMSEYG ERHSVARLIG APPGYVGYES
GGQLTEAVRR RPYTVVLFDE IEKAHQDVFD VLLQVLDEGR LTDGQGRTVD FRNTILILTS
NLGSGGSEEQ VMAAVRATFK PEFINRLDAV LIFDGLNPEE LVQIVDIQLE QLGKRLAQRR
LQLEVSLQAK RWLAQRGFDP VYGARPLRRL VQQAIGDQLA KMLLSGQVHD GDTVPVNVSP
DGDSLILG
//
