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Database: UniProt
Entry: A0A3A8F4L9_9GAMM
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ID   A0A3A8F4L9_9GAMM        Unreviewed;       859 AA.
AC   A0A3A8F4L9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034,
GN   ECO:0000313|EMBL:RKG35663.1};
GN   ORFNames=D7V21_01975 {ECO:0000313|EMBL:RKG35663.1};
OS   Acinetobacter guerrae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1843371 {ECO:0000313|EMBL:RKG35663.1, ECO:0000313|Proteomes:UP000269001};
RN   [1] {ECO:0000313|EMBL:RKG35663.1, ECO:0000313|Proteomes:UP000269001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCHAc060096 {ECO:0000313|EMBL:RKG35663.1,
RC   ECO:0000313|Proteomes:UP000269001};
RA   Qin J., Feng Y., Zong Z.;
RT   "The draft genome of Acinetobacter spp. strains.";
RL   Submitted (SEP-2018) 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:RKG35663.1}.
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DR   EMBL; RAXU01000002; RKG35663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3A8F4L9; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000269001; 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   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..458
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   859 AA;  95228 MW;  DD186D6B30C10699 CRC64;
     MRFEKFTNRL QQALSDAQSL ATGKDHTAID GVHILTVLLE EPSNLSLLQQ SGARLPELKQ
     KLEQALKDAP TIANPTGDVN LNPEAVKVLN LADRHAQKAG DEFLSTDWVL LALTETGSTK
     SLLNSVGVTT DALRKVIESI RGNDKVMSNN HEDQRDSLNK YTIDLTERAL AGKLDPVIGR
     DDEIRRTIQV LSRRTKNNPV LIGEPGVGKT AIVEGLAQRI VNGEVPESLK NKRVLSLDLG
     SLLAGAKYRG EFEERLKAVL NDLAKQDGNV ILFIDELHTL VGAGKTDGAM DAGNMLKPAL
     ARGELRCVGA TTLDEYRQYI EKDAALERRF QKVLVDEPSV EDTIAILRGL KEKYAAHHGV
     QILDSAIIAA AKMSHRYITD RQLPDKAIDL IDEAASRIKM EIDSKPEALD RLERRIIQLK
     MQLEAVKRDE DAGSKAEINH LEEQISIIEK EYNDMEEIWK AEKTLVEGDK KAQIELDHAR
     IAFDKAQREG DLAEAARLQY GVIPELQKRL EQAEVAEENE EPKLIRTKVT ENEIAEVVSA
     ATGIPVAKML QGEREKLLHM EEFLHNRVVG QDEAVVAVSN AVRRSRAGLS DPNRPSGSFL
     FLGPTGVGKT ELTKALANFL FDSDDAMIRI DMSEFMEKHS VSRLVGAPPG YVGYEEGGVL
     TEAVRRKPYS VVLFDEVEKA HPDVFNILLQ VLDDGRLTDS QGRVIDFKNT VIVMTSNLGS
     QDVRELGEGA TDDEVRAVVM SAVSQHFRPE FINRIDELVV FHSLKKSQIR GIADIQLDRL
     RSRLADREIG LTVDDTAFDI LIDAGFDPVY GARPLKRAIQ QQVENPLAQK ILGAEFQAGD
     NIIIKGDHGH LVFDKLKLS
//
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