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CLPB1_THEVB
ID   CLPB1_THEVB             Reviewed;         871 AA.
AC   Q8DJ40;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Chaperone protein ClpB 1;
GN   Name=clpB1; OrderedLocusNames=tlr1389;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(2002).
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; BA000039; BAC08941.1; -; Genomic_DNA.
DR   RefSeq; NP_682179.1; NC_004113.1.
DR   RefSeq; WP_011057229.1; NC_004113.1.
DR   AlphaFoldDB; Q8DJ40; -.
DR   SMR; Q8DJ40; -.
DR   STRING; 197221.22295113; -.
DR   PRIDE; Q8DJ40; -.
DR   EnsemblBacteria; BAC08941; BAC08941; BAC08941.
DR   KEGG; tel:tlr1389; -.
DR   PATRIC; fig|197221.4.peg.1461; -.
DR   eggNOG; COG0542; Bacteria.
DR   OMA; SKMMQGE; -.
DR   OrthoDB; 44062at2; -.
DR   Proteomes; UP000000440; Chromosome.
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..871
FT                   /note="Chaperone protein ClpB 1"
FT                   /id="PRO_0000191187"
FT   DOMAIN          6..147
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          9..73
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          84..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..550
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          560..771
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          772..871
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         610..617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   871 AA;  98389 MW;  D19D08E1A680F5FB CRC64;
     MQPSNPNQFT EKAWAAIART PDLAKQAQHQ NLESEHLMKS LLEQEGLATQ IFQKAGCSVQ
     RIRDLTDEFI SRQPKISHPS GVYLGQSLDK LLDRAEEARK QFGDEFISIE HLVLAFAQDD
     RFGKKLFQDI GLSEKVLREA IQQIRGSQKV TDQNPEGKYA ALEKYGRDLT LLARQGKLDP
     VIGRDDEIRR VIQILSRRTK NNPVLIGEPG VGKTAIAEGL AQRIVARDVP DSLRDRQLIA
     LDMGALIAGA KYRGEFEERL KAVLKEVTDS NGQIILFIDE IHTVVGAGAT QGAMDAGNLL
     KPMLARGELR CIGATTLDEY RKYIEKDAAL ERRFQQVYVD QPSVEDTISI LRGLKERYEI
     HHGVKISDTA LVAAATLSAR YISDRFLPDK AIDLVDEAAA KLKMEITSKP EELDEIDRKI
     LQLEMERLSL QKETSAASRD RLEKLERELA DLKEEQSRLN AQWQAEKEVI DRLQSIKEEI
     EKVNIEIQQA ERNYDLNRAA ELKYGKLTEL HKKLAEAEAK LREIQVGGRS LLRDEVTEAD
     IAEIISKWTG IPVSKLVESE AQKLLHLEEE LHKRVVGQDE AVSAVAEAIQ RSRAGLADPN
     RPIASFIFLG PTGVGKTELA KALAAFMFDT EEALVRIDMS EYMEKHAVSR LIGAPPGYVG
     YDEGGQLTEA IRRRPYAVVL FDEIEKAHPD VFNVFLQILD DGRVTDSQGR TVDFKNTIII
     MTSNIGSQYI LDVAGDDSRY SEMYNRVMEA MRAHFRPEFL NRVDEFIIFH SLRKDQLRQI
     VQLQVQRLQQ RLSDRHITLS LTEKAIDFLA EVGYDPVYGA RPLKRAIQKQ LETPIAKAIL
     RGDFFDGDTI LVDVGEDERL SFRRQVELAT V
 
 
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