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Database: UniProt
Entry: C4IDX3_CLOBU
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Original site: C4IDX3_CLOBU 
ID   C4IDX3_CLOBU            Unreviewed;       871 AA.
AC   C4IDX3;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 82.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:EEP55625.1};
GN   ORFNames=CLP_3553 {ECO:0000313|EMBL:EEP55625.1};
OS   Clostridium butyricum E4 str. BoNT E BL5262.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=632245 {ECO:0000313|EMBL:EEP55625.1, ECO:0000313|Proteomes:UP000003081};
RN   [1] {ECO:0000313|EMBL:EEP55625.1, ECO:0000313|Proteomes:UP000003081}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E4 str. BoNT E BL5262 {ECO:0000313|Proteomes:UP000003081};
RA   Shrivastava S., Brinkac L.B., Brown J.L., Bruce D.B., Detter C.,
RA   Green L.D., Munk C.A., Rogers Y.C., Tapia R., Sims D.R., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.;
RL   Submitted (AUG-2009) 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:EEP55625.1}.
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DR   EMBL; ACOM01000004; EEP55625.1; -; Genomic_DNA.
DR   RefSeq; WP_003408835.1; NZ_ACOM01000004.1.
DR   AlphaFoldDB; C4IDX3; -.
DR   STRING; 1492.ATN24_04555; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   Proteomes; UP000003081; 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   Reference proteome {ECO:0000313|Proteomes:UP000003081};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..149
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          415..495
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  98318 MW;  0D9A86EB585A5616 CRC64;
     MNVDKMTLRV QQALNDANAT AVKYTNSQID LIHLFSALVE QEDGLVPNIF TKMGVPVKNL
     ISSINAELDR LPKVTGEGLG NVYITRKVDE VLVKAEEISK KFEDSYVSVE HLMLAIMDVG
     KNTDVEKILK QYGVTKDSFL KVLSEVRGSQ RVETQDPEGT YDALAKYGTN LTDLAKKHKL
     DPVIGRDEEI RRTIRILSRR TKNNPVLIGE PGVGKTAIVE GLAERIVRGD VPEGLKDKII
     FSLDMGALIA GAKYRGEFEE RLKAVLKEVS NSDGRILLFI DEIHTIVGAG KTDGAMDAGN
     LIKPLLARGE LHCLGATTFD EYRQYIEKDK ALERRFQPVI VDEPSVDDTI AILRGLKERF
     EIHHGIRIHD SAIVAAAKLS DRYIQDRYMP DKAIDLIDEA GAMIRSEIDS LPTELDIVRR
     KIFKLEIEKE ALSKEKDEGS KKRLSDVEKE LAELKEKNDE MTAKYTKEKE NITSIKTLKS
     QLDEARGKIE EAQRNFDYNK VAEIQYSVIP KIEEEIKAKE AFTKENYEGA LLKEEVTEEE
     VSQVLAKWTG IPVSRLLEGE REKLLRLEED MSKRVIGQGE AVETVTNAIL RARAGLKDVN
     RPIGSFIFLG PTGVGKTELA KTLARNLFDS EENIIRIDMS EYMEKHSVSR LVGAPPGYVG
     YDEGGQLTEA VRRNPYSVIL FDEIEKAHED VFNIFLQILD DGRLTDNKGK TVDFKNTIII
     MTSNIGSEYL LENKNEDHVE DEIKSKVMTI LKSRFKPEFL NRVDDIIMFK PLTESGIKKI
     IDIFLKDVAR RLKDKNIIIE VTDEAETLMA REGYDPHYGA RPLKRYIQNT LENRLARMII
     KGELTYGSKV KIDGKDDEIT ITPIPTVAHL N
//
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