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 03-AUG-2022, entry version 98.
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; Proteobacteria; 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 PRIDE; Q7CU92; -.
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 OMA; SKMMQGE; -.
DR PhylomeDB; Q7CU92; -.
DR BioCyc; AGRO:ATU4177-MON; -.
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 Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 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; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
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
