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Database: UniProt
Entry: C7MLJ6_CRYCD
LinkDB: C7MLJ6_CRYCD
Original site: C7MLJ6_CRYCD 
ID   C7MLJ6_CRYCD            Unreviewed;       871 AA.
AC   C7MLJ6;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   13-SEP-2023, entry version 87.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Ccur_00690 {ECO:0000313|EMBL:ACU93802.1};
OS   Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS   12-3).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Cryptobacterium.
OX   NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU93802.1, ECO:0000313|Proteomes:UP000000954};
RN   [1] {ECO:0000313|EMBL:ACU93802.1, ECO:0000313|Proteomes:UP000000954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC   {ECO:0000313|Proteomes:UP000000954};
RX   PubMed=21304644; DOI=10.40456/sigs.12260;
RA   Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA   Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA   D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL   Stand. Genomic Sci. 1:93-100(2009).
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:RU362034}.
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DR   EMBL; CP001682; ACU93802.1; -; Genomic_DNA.
DR   RefSeq; WP_012802491.1; NC_013170.1.
DR   AlphaFoldDB; C7MLJ6; -.
DR   STRING; 469378.Ccur_00690; -.
DR   KEGG; ccu:Ccur_00690; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_11; -.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000000954; 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: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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362034};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU362034};
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:RU362034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000954};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..144
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          433..532
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   871 AA;  96474 MW;  CABBE7F5E6BB0CE3 CRC64;
     MRLDKLAITA QEALQVAMGI AGEHDNPTVE PIHLLAALID SNENNLEAII KRIGADAAQL
     RTLVSDEVEK LPHTQGSMSV PSNALLQVLD RAVKAAEKLG DSYATSEHVL IALSEDKGAA
     GRILSGQGVT RKNIEEAYEE LRGDTRVTEA DQKAEFEALE KYGQNLTQQA REGKLDPVIG
     RSEEIRRTVQ VLSRRTKNNP VLIGEPGVGK TAIVEGLAQR IVAGDVPTSL RDRDIIALDL
     GSMMAGAKYR GEFEDRLKAV LREVKDAEGR IILFIDELHT IVGAGSTGDS SLDAGNMLKP
     ALARGELHAI GATTLDEYHK YIEKDAALER RFQPVIVGEP TVEDTIAILR GLKEKYEIHH
     GVRITDNALV AAAELSNRYI SDRFLPDKAI DLMDEAASRL RIEIDSMPEE VDLASRKLTQ
     MQIEEQALMK EGDAASKERL AALQQEIASA QEDLDKRKAE WKNEKDVIVR VQELKSELEA
     AQSEEERATR EGDLSRASEL RYARIPELKN QLADAETELN AKQQDGAILK EEVSEEEIAE
     VVSTWTGIPV SKMMQGEMAK LADLEDRLHE RVVGQDEAVS AVAGAIRRNR AGLSDPDRPI
     GSFLFLGPTG VGKTELAKAL AEYLFDTERA MVRIDMSEYM EKFSVQRLIG APPGYVGYDE
     GGQLTEAVRR RPYSVILLDE IEKAHPDVFN ILLQVLDDGR LTDGQGRVVS FKNAIIIMTS
     NVGSQFIREF AENGDEKQMR EAIDDALRQT FRPEFINRID DVVVFNSLSF NAIEPIVDLQ
     LEDVRDRLAQ RRIQLEVKPD AMQQLALDGY DPVFGARPLK RLIQKEIVDR VANEIVRGHV
     LDGSKVVISL DDELHYHCTV EEPAGQPELG V
//
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