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
//