ID A0A0Q9ZT90_9GAMM Unreviewed; 865 AA.
AC A0A0Q9ZT90;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=AK824_08525 {ECO:0000313|EMBL:KRG35417.1};
OS Psychrobacter sp. P11G3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1699623 {ECO:0000313|EMBL:KRG35417.1, ECO:0000313|Proteomes:UP000051518};
RN [1] {ECO:0000313|EMBL:KRG35417.1, ECO:0000313|Proteomes:UP000051518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P11G3 {ECO:0000313|EMBL:KRG35417.1,
RC ECO:0000313|Proteomes:UP000051518};
RA Ruckert C., Albersmeier A., Moghadam M.S., Winkler A., Lale R.,
RA Kalinowski J.;
RT "High quality draft genome sequence of Psychrobacter sp. P11G3, isolated
RT from an ascidian tunicate in the Norwegian sea.";
RL Submitted (AUG-2015) 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:KRG35417.1}.
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DR EMBL; LJCF01000002; KRG35417.1; -; Genomic_DNA.
DR RefSeq; WP_057760702.1; NZ_CM003596.1.
DR AlphaFoldDB; A0A0Q9ZT90; -.
DR STRING; 1699623.AK824_08525; -.
DR PATRIC; fig|1699623.3.peg.1775; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000051518; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 78, MITOCHONDRIAL; 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 Hydrolase {ECO:0000313|EMBL:KRG35417.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:KRG35417.1};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..143
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 409..489
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 865 AA; 95977 MW; D061575E00B52584 CRC64;
MRFEKFTQKL QSAIQEAQSL ALGRDHTGID PVHLLAVLLQ DESNLSICQQ AGASIPALKN
GVAKALDNQA TISEPTGDVN LNPNSVKILN LADRQAQKEG DDFIATEWVM LALAEQGETK
KIFESAGVTA SKLKEVIEQL RGDDTVNNQN AEDQRDALNK YTINLTEQAE LGKLDPVIGR
DEEIRRTIQV LSRRTKNNPV LIGEPGVGKT AIVEGLAQKI INGDVPEGLR RKEVLSLDLG
ALIAGAKFRG EFEERLKSVL SDLAKQEGNV ILFIDELHTM VGAGKSEGAM DAGNMLKPAL
ARGELHCVGA TTLDEYRKYI EKDAALERRF QKVLVDEPTV EDTIAILRGL KERYELHHGV
DIQDSAIIAA ARMSHRYITD RKLPDKAIDL IDEAASRLRM EMDSKPESLG KLDSRLIQLK
MQREVLKNEE DAGAQAERKV LDAQIAELEK EYADLNEVWQ AEKALVKGSQ QLKDELDKAR
IAYDKASREG DYETMSKLQY ETIPQLERRI HESDLAEQKE QTGEGSGVKL LRNKVTDNEI
AEVVAAATGI PVSKMMQGER DKMIAMEEKL HERVIGQNEA VESVANAVRR SRAGLSDPNR
PSGSFLFLGP TGVGKTELTK SLANFLFDSE DAIVRIDMSE YMEKHSVSRL VGAPPGYVGY
EEGGTLTEAV RRKPYSVILF DEVEKAHPDV FNILLQVLDD GRLTDSQGRV VDFKNTVIIM
TSNLGSHKIQ EMVGESYEDI KAEVMDSVGQ HFRPEFVNRI DEIVVFHPLG MSQMAGIADI
QLDRLRQRIQ EREMDIELSA DAMNKLVAVG YDPVYGARPL KRAIQQEIEN PLSLKLLAGD
FVAGDIIKVD VGADDKLTFD KLRMS
//
