GenomeNet

Database: UniProt
Entry: A0A1A9RY39_9NEIS
LinkDB: A0A1A9RY39_9NEIS
Original site: A0A1A9RY39_9NEIS 
ID   A0A1A9RY39_9NEIS        Unreviewed;       857 AA.
AC   A0A1A9RY39;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|ARBA:ARBA00017574, ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=A7P95_04540 {ECO:0000313|EMBL:OAM29218.1};
OS   Eikenella longinqua.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Eikenella.
OX   NCBI_TaxID=1795827 {ECO:0000313|EMBL:OAM29218.1, ECO:0000313|Proteomes:UP000077885};
RN   [1] {ECO:0000313|Proteomes:UP000077885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML02-A-017 {ECO:0000313|Proteomes:UP000077885};
RA   Bernier A.-M., Bernard K.;
RT   "Draft genome of Corynebacterium afermentans subsp. afermentans LCDC
RT   88199T.";
RL   Submitted (MAY-2016) 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:OAM29218.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LXSL01000016; OAM29218.1; -; Genomic_DNA.
DR   RefSeq; WP_067591839.1; NZ_LXSL01000016.1.
DR   AlphaFoldDB; A0A1A9RY39; -.
DR   STRING; 1795827.A7P95_04540; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000077885; 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..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          441..492
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   857 AA;  94855 MW;  398CEB4266A137C0 CRC64;
     MRFDKLTAKF QQALQEGQSL ALAADSSYLE AGFVLKALLD DQNSGAAALL AHAGVNVPQV
     KQRLQQQLSS LPKVSGQGGD MVPSRELQAV LNLMDKAAIK RGDAYIASEL FLLALVQQND
     ATGKILKEAG ATEQNINAAI DAVRGGQNVN DANAEDQREA LKKYTTDLTQ RARDGKLDPV
     IGRDDEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLRNKRLLVL
     DLAALIAGAK YRGEFEERLK AVLNELSKDD GNTLIFIDEI HTLVGAGKTD GAMDASNMLK
     PALSRGELHC IGATTLDEYR QYIEKDAALE RRFQKVLVGE PSVEDTIAIL RGLQERYEIH
     HGIDITDPAI VAAAELSDRY ITDRFLPDKA IDLIDEAASR IKMELDSKPE QMDKLDRRII
     QLKMEKMHVA KESDDASKKR LELIDEEIDG LQKEYADLDE IWKAEKAASS STADIKKQMD
     DIKVKIEQAK RQGDFARASE LEYGELPKLG AQLQAAESNA DGKKQNKLFR TEVGADEVAE
     IVSRMTGIPV SKMMEGERDK LLKMEEVLHR RVVGQDEAVR AVSDAIRRSR SGLADPNKPY
     GSFLFLGPTG VGKTELCKAL AGFLFDSEDH LIRIDMSEYM EKHAVARLIG APPGYVGYEE
     GGYLTEQVRR KPYSVILLDE VEKAHPDVFN ILLQVLDDGR LTDGQGRTVD FKNTVIVMTS
     NIGSQHIQQM GTDDYEAVKE VVMEDVKTHF RPEMINRIDE VVVFHGLDQA NIRSIAKIQL
     KGLEKRLEKQ NLRLSVSDAA LDIIAKAGFD PIYGARPLKR AIQSEIENPL AKALLEGRYV
     PESTIKVEAD GDRLVFA
//
DBGET integrated database retrieval system