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Database: UniProt
Entry: CLPB_AGRFC
LinkDB: CLPB_AGRFC
Original site: CLPB_AGRFC 
ID   CLPB_AGRFC              Reviewed;         874 AA.
AC   Q7CU92; Q8U8B5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=Atu4177; ORFNames=AGR_L_1346;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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. Acts before DnaK, in the
CC       processing of protein aggregates. Protein binding stimulates the ATPase
CC       activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC       which probably helps expose new hydrophobic binding sites on the
CC       surface of ClpB-bound aggregates, contributing to the solubilization
CC       and refolding of denatured protein aggregates by DnaK (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC       discriminating domain, recruiting aggregated proteins to the ClpB
CC       hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC       responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC       hexamer probably in an ATP-dependent manner. The movement of the
CC       coiled-coil domain is essential for ClpB ability to rescue proteins
CC       from an aggregated state, probably by pulling apart large aggregated
CC       proteins, which are bound between the coiled-coils motifs of adjacent
CC       ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; AE007870; AAK89256.2; -; Genomic_DNA.
DR   PIR; AC3070; AC3070.
DR   PIR; F98216; F98216.
DR   RefSeq; NP_356471.2; NC_003063.2.
DR   RefSeq; WP_010973618.1; NC_003063.2.
DR   AlphaFoldDB; Q7CU92; -.
DR   SMR; Q7CU92; -.
DR   STRING; 176299.Atu4177; -.
DR   EnsemblBacteria; AAK89256; AAK89256; Atu4177.
DR   GeneID; 66224417; -.
DR   KEGG; atu:Atu4177; -.
DR   PATRIC; fig|176299.10.peg.3991; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_1_5; -.
DR   OrthoDB; 9803641at2; -.
DR   PhylomeDB; Q7CU92; -.
DR   BioCyc; AGRO:ATU4177-MONOMER; -.
DR   Proteomes; UP000000813; Chromosome linear.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
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; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW   Reference proteome; Repeat; Stress response.
FT   CHAIN           1..874
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191084"
FT   DOMAIN          3..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          6..71
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          83..147
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          160..341
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          342..547
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          557..767
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          768..874
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          392..526
FT                   /evidence="ECO:0000250"
FT   BINDING         207..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         607..614
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   874 AA;  96340 MW;  73A9ABBBE53B7C17 CRC64;
     MNIDKYSERV RGFLQSAQTF ALAENHQQFS PEHVLKVLLD DEQGMAASLI ERAGGDAKEA
     RLANDAALAK LPKVSGGNGG LSLTAPLAKV FSTAEDLAKK AGDSFVTVER LLQALAIESS
     ASTSASLKKA GATAQALNQV INDIRKGRTA DSANAEQGFD ALKKYARDLT EEAREGRLDP
     VIGRDDEIRR TIQVLSRRTK NNPVLIGEPG VGKTAIAEGL ALRIVNGDVP ESLKDKKLMA
     LDMGALIAGA KYRGEFEERL KAVLNEVQAE NGGIILFIDE MHTLVGAGKA DGAMDASNLL
     KPALARGELH CVGATTLDEY RKHVEKDPAL ARRFQPVLVD EPNVEDTISI LRGLKEKYEQ
     HHKVRISDSA LVAAATLSNR YITDRFLPDK AIDLMDEAAS RLRMQVDSKP EELDELDRRI
     IQLKIEREAL KQETDQSSVD RLRKLEDELA DTEEKADALT ARWQAEKQKL GHAADLKKRL
     DEARNELAIA QRNGQFQRAG ELTYGIIPGL EKELAAAEAR DSSGAGSMVQ EVVTPDNIAH
     VVSRWTGIPV DKMLEGQREK LLRMEDELAK SVVGQGEAVQ AVSKAVRRSR AGLQDPNRPI
     GSFIFLGPTG VGKTELTKSL ARFLFDDETA MVRLDMSEYM EKHSVARLIG APPGYVGYEE
     GGALTEAVRR RPYQVVLFDE IEKAHPDVFN VLLQVLDDGR LTDGQGRTVD FKNTIIIMTS
     NLGSEFMTQM GDNDDVDSVR ELVMERVRSH FRPEFLNRID DIILFHRLRR DEMGAIVEIQ
     LKRLVSLLAD RKITLELDED ARSWLANKGY DPAYGARPLK RVIQKSVQDR LAEMILGGEI
     PDGSRVKVTS GTDRLLFKVK PAKGEAETET ADAA
//
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