(data stored in SCRATCH zone)

SWISSPROT: A1AY35_PARDP

ID   A1AY35_PARDP            Unreviewed;       875 AA.
AC   A1AY35;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 109.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Pden_0062 {ECO:0000313|EMBL:ABL68179.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68179.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) 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.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|SAAS:SAAS00721915}.
CC   -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC       {ECO:0000256|RuleBase:RU362034}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034,
CC       ECO:0000256|SAAS:SAAS00738470}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|RuleBase:RU004432, ECO:0000256|SAAS:SAAS01144294}.
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DR   EMBL; CP000489; ABL68179.1; -; Genomic_DNA.
DR   RefSeq; WP_011746412.1; NC_008686.1.
DR   STRING; 318586.Pden_0062; -.
DR   PRIDE; A1AY35; -.
DR   EnsemblBacteria; ABL68179; ABL68179; Pden_0062.
DR   KEGG; pde:Pden_0062; -.
DR   eggNOG; ENOG4105C2Z; Bacteria.
DR   eggNOG; COG0542; LUCA.
DR   HOGENOM; HOG000218211; -.
DR   KO; K03695; -.
DR   OMA; HHKVRIK; -.
DR   BioCyc; PDEN318586:G1GW1-63-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019538; P:protein metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR017730; Chaperonin_ClpB.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR004176; Clp_N.
DR   InterPro; IPR036628; Clp_N_dom_sf.
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; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AY35.
DR   SWISS-2DPAGE; A1AY35.
KW   ATP-binding {ECO:0000256|RuleBase:RU004432,
KW   ECO:0000256|SAAS:SAAS01144309};
KW   Chaperone {ECO:0000256|RuleBase:RU004432,
KW   ECO:0000256|SAAS:SAAS00127789};
KW   Coiled coil {ECO:0000256|RuleBase:RU362034};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Cytoplasm {ECO:0000256|RuleBase:RU362034,
KW   ECO:0000256|SAAS:SAAS00738398};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004432,
KW   ECO:0000256|SAAS:SAAS01144287};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Repeat {ECO:0000256|SAAS:SAAS00983801};
KW   Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN      198    344       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      595    765       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      764    853       ClpB_D2-small. {ECO:0000259|SMART:
FT                                SM01086}.
FT   COILED      434    461       {ECO:0000256|RuleBase:RU362034}.
FT   COILED      469    499       {ECO:0000256|RuleBase:RU362034}.
SQ   SEQUENCE   875 AA;  96245 MW;  FCD5735988F54918 CRC64;
     MDMEKFTERS RGFLQAAQTI AIREENQRVM PEHLLKALMD DDQGFASNLI ARAGGDAQAV
     RQAVDQAVEK QPKVSGGQGQ VYIDPSMVRV LDEAEKLAKK AGDSFVPAER VLTALAIVNT
     NARDALAAGK VTAQALNSAI NDVRKGRTAD TASAEDSYEA LSKYARNLTE AAAEGKIDPI
     IGRDEEIRRA MQVLSRRTKN NPVLIGEPGV GKTAIAEGLA LRIVDGDVPE SLRNKQLWAL
     DMGALIAGAK YRGEFEERLK SVLKEIENAA GEIVLFIDEL HVLVGAGKTD GAMDAANLIK
     PALARGELHC VGATTLDEYR KYIEKDAALA RRFQPVMIEE PTVEDTISIL RGIKEKYELH
     HGVRISDAAL VAAATLSHRY ITDRFLPDKA IDLMDEAASR LRMEVDSKPE ELDALDRQIL
     QMQIEAEALK KEDDAASQDR LEKLEKQLSE LQEKSATMTA RWQAERDKLE GSRNLKEQLD
     RARAELDQAK REGNLARAGE LSYGIIPGLE RQLAESEGSE DGPMVEEAVR PEQIAEVVER
     WTGIPTSKML EGEREKLLKM EDVLSKRVIG QSEAVTAISN AVRRARAGLN DPKRPLGSFL
     FLGPTGVGKT ELTKAIAEYL FDDDSAMVRI DMSEFMEKHS VARLIGAPPG YVGYDEGGVL
     TEAVRRRPYQ VILFDEVEKA HPDVFNVLLQ VLDDGQLTDG QGRTVDFKQT LIVLTSNLGA
     QALSALPEGA DSGQARAQVM DAVRAHFRPE FLNRLDEIII FHRLTRENMD GIVRIQLWQL
     ETRLAQHKIG LDLDEAALKW LADEGYDPVF GARPLKRVMQ RSLQNPLAEM ILAGEVLDGQ
     TVHVSAGPDG LIVGNRVSTA HLGPADESGP RVPLH
//

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