ID F2BED9_9NEIS Unreviewed; 857 AA.
AC F2BED9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 72.
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:EGF10220.1};
GN ORFNames=HMPREF9123_2095 {ECO:0000313|EMBL:EGF10220.1};
OS Neisseria bacilliformis ATCC BAA-1200.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=888742 {ECO:0000313|EMBL:EGF10220.1, ECO:0000313|Proteomes:UP000004105};
RN [1] {ECO:0000313|EMBL:EGF10220.1, ECO:0000313|Proteomes:UP000004105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1200 {ECO:0000313|EMBL:EGF10220.1,
RC ECO:0000313|Proteomes:UP000004105};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (FEB-2011) 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:EGF10220.1}.
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DR EMBL; AFAY01000044; EGF10220.1; -; Genomic_DNA.
DR RefSeq; WP_007343101.1; NZ_GL878494.1.
DR AlphaFoldDB; F2BED9; -.
DR STRING; 267212.GCA_001063965_00187; -.
DR HOGENOM; CLU_005070_4_0_4; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000004105; 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:UP000004105};
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; 94654 MW; 8766CCDB7DDB5BA5 CRC64;
MRFDKLTAKF QQALQEGQSL ALAADSSYLE AGFVLKALLD DQNSGAAALL AHAGVNVPQV
KQKLAAHLNG LPKVSGQGGD IMPSRELQAV LNLMDKAAVK RGDAYIASEL FLLALVQQND
ATGKILKEAG ATEQNINAAI DAVRGGQNVN DANAEDQRDA LKKYTLDLTQ RARDGKLDPV
IGRDDEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLRNKRLLVL
DLAALIAGAK YRGEFEERLK GVLNDLAKDD GNTLIFIDEI HTLVGAGKTD GAMDAGNMLK
PALARGELHC IGATTLDEYR QYIEKDAALE RRFQKVLVGE PSVEDTIAIL RGLQERYEIH
HGIDITDPAI VAAAELSDRY ITDRFLPDKA IDLIDEAASR IKMELDSKPE QMDKLDRRII
QLKMEKMHVA KESDDASKKR LELIDEEIDG LQKEYADLDE IWKAEKAASS STADIKKQMD
DIKVKIEQAK RQGDFARASE LEYGELPKLG QQLQAAESNP EGKKANKLFR TEVGADEVAE
IVSRMTGIPV AKMMEGERDK LLKMEEVLHR RVVGQDEAVR AVSDAIRRSR SGLADPNKPY
GSFLFLGPTG VGKTELCKAL AGFLFDSEDH LIRIDMSEYM EKHAVARLIG APPGYVGYEE
GGYLTEQVRR KPYSVILLDE VEKAHPDVFN ILLQVLDDGR LTDGQGRTVD FKNTVIVMTS
NIGSQHIQQM GTQDYEAVKE AVMEEVKAYF RPEMINRIDE VVVFHGLNQE NIRNIAKIQL
KGLEKRLEAQ HLHLKVDDAA LDLIAKAGFD PVYGARPLKR AIQSEIENPL AKALLEGRYA
PESTIHVGVE NGRLAFA
//