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Database: UniProt
Entry: Q2RWD8_RHORT
LinkDB: Q2RWD8_RHORT
Original site: Q2RWD8_RHORT 
ID   Q2RWD8_RHORT            Unreviewed;       870 AA.
AC   Q2RWD8;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Rru_A0753 {ECO:0000313|EMBL:ABC21557.1};
OS   Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 /
OS   NCIMB 8255 / S1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=269796 {ECO:0000313|EMBL:ABC21557.1, ECO:0000313|Proteomes:UP000001929};
RN   [1] {ECO:0000313|EMBL:ABC21557.1, ECO:0000313|Proteomes:UP000001929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1
RC   {ECO:0000313|Proteomes:UP000001929};
RX   PubMed=21886856; DOI=10.4056/sigs.1804360;
RA   Munk A.C., Copeland A., Lucas S., Lapidus A., Del Rio T.G., Barry K.,
RA   Detter J.C., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Kyrpides N.C.,
RA   Mavromatis K., Richardson P., Rohde M., Goker M., Klenk H.P., Zhang Y.,
RA   Roberts G.P., Reslewic S., Schwartz D.C.;
RT   "Complete genome sequence of Rhodospirillum rubrum type strain (S1).";
RL   Stand. Genomic Sci. 4:293-302(2011).
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.
CC       {ECO:0000256|ARBA:ARBA00025613}.
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|ARBA:ARBA00004496,
CC       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; CP000230; ABC21557.1; -; Genomic_DNA.
DR   RefSeq; WP_011388511.1; NC_007643.1.
DR   RefSeq; YP_425844.1; NC_007643.1.
DR   AlphaFoldDB; Q2RWD8; -.
DR   STRING; 269796.Rru_A0753; -.
DR   EnsemblBacteria; ABC21557; ABC21557; Rru_A0753.
DR   KEGG; rru:Rru_A0753; -.
DR   PATRIC; fig|269796.9.peg.806; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_5; -.
DR   OMA; ERMKAVM; -.
DR   PhylomeDB; Q2RWD8; -.
DR   Proteomes; UP000001929; 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:UP000001929};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          412..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   870 AA;  95557 MW;  2A5979C40CE538C3 CRC64;
     MDPEKLTDRS KGFLQAAQTI ALRETHQQVT PEHLLKALLD DKEGLAANLI RAAGGDPLRA
     QEAVNREVDK LPKVQGAQQM YWAQSLARVI DQATRMAEKA GDSFVTVERL LIALAMAAET
     PAKRILAEAG ATPQGLNKAV EDLRKGRKAD SAGAESQYDA LKKYARDLTE AAREGKLDPV
     IGRDEEIRRT IQVLSRRTKN NPVLIGEPGV GKTAIIEGLA LRIVNGDVPE SLQNKKLMAL
     DLGAMVAGAK FRGEFEERLK AMLTEVSAAE GEIILFIDEM HTLIGAGAGE GAMDASNLLK
     PALARGDLHC VGATTLNEYR KHVEKDAALA RRFQPVFVSE PGVADTISIL RGIKEKYELH
     HGVRIADNAL VAAATLSNRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ALDELDRRII
     QLKIEREALR KEKDIASEAR LSDLEKELAD LESQSATLTE DWKREKEGLA GSTRIKEQLE
     QARGDLDIAK RQANWARAGE LEYGVIPDLE RRLGEVESGD GLAHRQGGKL VNEVVTAETI
     ASVVSRWTGI PVDKMLAGER EKLLGMEKVL ASRVVGQREA VVAVSNAVRR SRAGLQDPNR
     PMGSFLFLGP TGVGKTELTK ALAAFLFDDE QAMVRIDMSE YMEKHAVSRL IGAPPGYVGY
     DEGGALTEAV RRRPYQVILF DEVEKAHPDV FNVLLQVLDD GRLTDGQGRT VDFRNTLIVL
     TSNLGADILA NQPEGDDSGA VRGAVMEMVR AAFRPEFLNR LDEILLFHRL FRENMAGIVS
     IQLGRLADRL RDRKMTLDLD DAARDWLAER GYDPVYGARP LKRVIQRSLE NPLATLVLDG
     RIKDGDVIRI TVEGGKLVVN GEALSLDTAA
//
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