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Database: UniProt
Entry: F2BED9_9NEIS
LinkDB: F2BED9_9NEIS
Original site: F2BED9_9NEIS 
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
//
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