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
//