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Database: UniProt
Entry: S6HCK0_9GAMM
LinkDB: S6HCK0_9GAMM
Original site: S6HCK0_9GAMM 
ID   S6HCK0_9GAMM            Unreviewed;       930 AA.
AC   S6HCK0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=OFPII_22400 {ECO:0000313|EMBL:EPJ46213.1};
OS   Osedax symbiont Rs1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae.
OX   NCBI_TaxID=1330036 {ECO:0000313|EMBL:EPJ46213.1, ECO:0000313|Proteomes:UP000014822};
RN   [1] {ECO:0000313|EMBL:EPJ46213.1, ECO:0000313|Proteomes:UP000014822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rs1 {ECO:0000313|Proteomes:UP000014822};
RA   Yi H., Goffredi S.;
RT   "Comparative genomics of two novel heterotrophic symbionts of deep-sea
RT   Osedax worms: functional variation and environmental selection.";
RL   Submitted (MAY-2013) 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. {ECO:0000256|RuleBase:RU362034}.
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|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPJ46213.1}.
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DR   EMBL; ASZJ01000105; EPJ46213.1; -; Genomic_DNA.
DR   AlphaFoldDB; S6HCK0; -.
DR   PATRIC; fig|1330036.3.peg.2140; -.
DR   Proteomes; UP000014822; Unassembled WGS sequence.
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:UP000014822};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          75..217
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          476..563
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   930 AA;  103686 MW;  A4D8F8B121AA9ADC CRC64;
     MTSLRHIAQA LDSTAVRKIP AEPTGAAKIF QFHCRTNILH SVFTLKSRIQ VEVIQKRSLL
     NKNPIIWIEE QSMRPEKFTA KLQQAIADAQ SLAIDKQHNL IEPVHLLSVF INEQPSAINA
     LLANLINLPS LQAAVSVAVD NLPRLNSLDC DVRLAQSCSR LFASAEKLAE RRGDQFIATE
     IVLQAMLDDK TVVAKLLKQA SINKTNLTQA IDALRAGDSV KDANAEDNRQ SLDKYCIDLT
     ELAEQGKLDP VIGRDDEIRR TIQVLQRRTK NNPVLIGEPG VGKTAIVEGL AQRIVNAEVP
     EGLKNKRVLS LDMAALIAGA KFRGEFEERL KAVLKELQKA EGQIILFIDE LHTMVGAGGG
     EGSMDAGNML KPALARGDLH CVGATTLDEY RKYVEKDAAL ERRFQKVLVD QPDEQSTVAI
     LRGLKGRYEV HHGVDITDSA IIAAVKLSQR YITDRQLPDK AIDLIDEAAS GIRLEMDSKP
     EELDKLERKI IQLKMEREAL KKERDAAAKQ RLKELLLSLA ELEKSFANLE EIWLAEKAVL
     QRSQQIKEQL DQARIDMEQA SRAGDLNKMS EIQYGVIPDL EKQLLIAAQA EQSAEQSNQL
     LRNKVTEEEV AEVVARWTGI PVHKMLQGER EKLLVMEQEL QKTVIGQSAA VLAVANAVRR
     SKAGLSDPNR PNGSFLFLGP TGVGKTELCK TLAQYLFDTK EAMVRIDMSE FMEKHSVARL
     IGAPPGYVGY EEGGYLTEAV RRKPYSVLLL DEVEKAHPDV FNILLQVLED GRLTDGQGRT
     VDFRNTIVVM TSNLGSQQIQ NVSAHADYQQ MRSAVMEEVT NFFRPEVLNR IDEIVVFKRL
     EKPEVAQIAK IQLAYLQQRL ADKDLSLRVT DEAMEHLVEL GYEPMYGARP LKRAIQQWIE
     NPLAEALLAG RYVPGSEVVV ALAEGQFVFN
//
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