ID A0A0J5GIW4_9NEIS Unreviewed; 858 AA.
AC A0A0J5GIW4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034};
GN ORFNames=ACG97_04170 {ECO:0000313|EMBL:KMJ54286.1};
OS Vogesella sp. EB.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Vogesella.
OX NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ54286.1, ECO:0000313|Proteomes:UP000054352};
RN [1] {ECO:0000313|EMBL:KMJ54286.1, ECO:0000313|Proteomes:UP000054352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EB {ECO:0000313|EMBL:KMJ54286.1,
RC ECO:0000313|Proteomes:UP000054352};
RA Arrua Day P., Revale S., Alvarez H.M.;
RT "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT Vogesella sp. strain EB.";
RL Submitted (JUN-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. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000256|ARBA:ARBA00025613}.
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:KMJ54286.1}.
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DR EMBL; LFDT01000004; KMJ54286.1; -; Genomic_DNA.
DR RefSeq; WP_047966069.1; NZ_LFDT01000004.1.
DR AlphaFoldDB; A0A0J5GIW4; -.
DR STRING; 1526735.ACG97_04170; -.
DR PATRIC; fig|1526735.3.peg.892; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000054352; 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:UP000054352};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT COILED 412..492
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COILED 774..801
FT /evidence="ECO:0000256|RuleBase:RU362034"
SQ SEQUENCE 858 AA; 94670 MW; 3E15D749D380E394 CRC64;
MRFDKLTTKF QQALGDSQSL ALAGDNAYIE PQHLLLAMLD DADSGIVSLL ARAGVNVSAL
KGSLRDAVAR LPKVSGTGGE VTVSRDLTNL LNLADKAAMK RGDQFIASEL FLLVLAEDKG
ETGRLLKQHG GNSAAIHAAV EAVRGGDAVN SADAEEQREA LKKYTLDLTE RARQGKLDPV
IGRDDEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLKHKKLLVL
DMAGLIAGAK FRGEFEERLK AVLSDIAKDE GSIILFIDEI HTMVGAGKAE GAMDAGNMLK
PALARGELHC LGATTLDEYR KYIEKDAALE RRFQKVLVDE PTVEDTIAIL RGLQEKYEIH
HGVDITDPAI VAAAELSHRY ITDRFLPDKA IDLIDEAASK IKMELDSKPE EMDKLDRRLI
QLKIEREAVK RETDEASKKR LQLIEEEIGG LSREYADLEE IWKAEKASQQ GSQSIKEEIE
RLKVEMDELK RKGDWQKLAE LQYGKLPQLE GRLKDAEAAA SGDNKPNRLL RTQVGAEEIA
EVISRMTGIP VSKMLTGERE KLLHMEAVLH QRVVGQDEAV TVVADAIRRS RSGLADPNRP
YGSFLFLGPT GVGKTELCKA LAGFLFDSEE HLIRVDMSEY MEKHSVARLI GAPPGYVGYE
EGGMLTEQVR RKPYSVILLD EVEKAHPDVF NVLLQVLDDG RLTDGQGRTV DFKNTVIVMT
SNMGSQHIQA MASDDYQVVK LAVLAEVKSH FRPEFVNRID ELVVFHALAE AQIKSIARIQ
LKRLEQRLAK LELNLQVSEE ALSLIADAGF DPVYGARPLK RAIQSEIENP LAKAILAGHY
LPKATVMVDV RGGQLVFD
//