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Database: UniProt
Entry: R4KMF2_9FIRM
LinkDB: R4KMF2_9FIRM
Original site: R4KMF2_9FIRM 
ID   R4KMF2_9FIRM            Unreviewed;       863 AA.
AC   R4KMF2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=Desgi_3393 {ECO:0000313|EMBL:AGL02737.1};
OS   Desulfoscipio gibsoniae DSM 7213.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC   Desulfoscipio.
OX   NCBI_TaxID=767817 {ECO:0000313|EMBL:AGL02737.1, ECO:0000313|Proteomes:UP000013520};
RN   [1] {ECO:0000313|EMBL:AGL02737.1, ECO:0000313|Proteomes:UP000013520}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7213 {ECO:0000313|EMBL:AGL02737.1,
RC   ECO:0000313|Proteomes:UP000013520};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Parshina S.,
RA   Plugge C., Muyzer G., Kuever J., Ivanova A., Nazina T., Klenk H.-P.,
RA   Brambilla E., Spring S., Stams A.F., Woyke T.;
RT   "Complete sequence of Desulfotomaculum gibsoniae DSM 7213.";
RL   Submitted (JAN-2012) 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; CP003273; AGL02737.1; -; Genomic_DNA.
DR   RefSeq; WP_006523398.1; NC_021184.1.
DR   AlphaFoldDB; R4KMF2; -.
DR   STRING; 767817.Desgi_3393; -.
DR   KEGG; dgi:Desgi_3393; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000013520; 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; 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:UP000013520};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          413..527
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   863 AA;  96462 MW;  B6B024560FE53ADB CRC64;
     MDINRYTQKS REALSAAQQL AAARHHQEVT GKHLLAALLA QDGGMVPRFV EHAGASLVNL
     TGQVDALLKK IPVVTGYEGS LHLGGGLVRV LARAEKEARD MKDDYISVEH LLLALLEEGE
     PETRDALRQS GLTRDALLNS LRAVRGNQRV TGENPEETYE ALERYGRDLT KLAAEGKLDP
     VIGRDNEIRR AMEILSRRTK NNPVLIGEPG VGKTAIVEGL ARRIVAGDVP EGLKEKRIIG
     LDMGSLLAGA KYRGEFEERL KAVLKEVQQS QGRIILFIDE LHTVVGAGKA EGAVDAGNIL
     KPMLARGELR TIGATTLDEY RKHVEKDAAL ERRFQPVQVQ PPSVEDTISI LRGLKERYEV
     HHGVRIQDSA LVASATLSDR YISDRFLPDK AIDLMDEAAA RLRTEIDSMP AELDEITRRI
     MQLEIEEAAL SKETDPASKE RLNKIKAQLA ELREESGAMQ AQWQVEKQAI SRVRQLKKEI
     EETRQEIERA ERDYDLNRLA ELKYGRLNEL ERRLKSEEEH LAGKQKHGML LKEEVDEEDI
     ARVVSRWTGI PVSKLMEGER EKLIHLDEEL HKRVVGQDEA VRAVADAVLR ARAGIKDPNR
     PIGSFIFLGP TGVGKTELAR ALAQALFDDE RNMTRLDMSE YMEKHTVARL IGAPPGYVGY
     EEGGQLTEAV RRKPYSVILL DEIEKAHPDV FNVLLQLLED GRLTDGQGRT VNFQNTVVIM
     TSNLGSHEIL AQQERGSDFD KMKTAVLGIL RQHFRPEFLN RVDEIVVFHA LSQSQVRQIA
     GLLLERLARR IYAGTGIKLT WDDSALNYLA GKGYEPAYGA RPLKRVIQQL VETALSRMII
     RGEVGPQQTV TLQVEDGELH IIA
//
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