ID   CLPB_NEIMA              Reviewed;         859 AA.
AC   Q9JTP9; A1ISQ2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Chaperone protein ClpB;
GN   Name=clpB; OrderedLocusNames=NMA1683;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC       discriminating domain, recruiting aggregated proteins to the ClpB
CC       hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC       responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC       hexamer probably in an ATP-dependent manner. The movement of the
CC       coiled-coil domain is essential for ClpB ability to rescue proteins
CC       from an aggregated state, probably by pulling apart large aggregated
CC       proteins, which are bound between the coiled-coils motifs of adjacent
CC       ClpB subunits in the functional hexamer (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR   EMBL; AL157959; CAM08814.1; -; Genomic_DNA.
DR   PIR; F81863; F81863.
DR   RefSeq; WP_002247010.1; NC_003116.1.
DR   AlphaFoldDB; Q9JTP9; -.
DR   SMR; Q9JTP9; -.
DR   PRIDE; Q9JTP9; -.
DR   EnsemblBacteria; CAM08814; CAM08814; NMA1683.
DR   KEGG; nma:NMA1683; -.
DR   HOGENOM; CLU_005070_4_0_4; -.
DR   OMA; SKMMQGE; -.
DR   BioCyc; NMEN122587:NMA_RS08445-MON; -.
DR   Proteomes; UP000000626; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   Gene3D; 1.10.1780.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 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   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; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF81923; SSF81923; 1.
DR   TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
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; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding; Repeat;
KW   Stress response.
FT   CHAIN           1..859
FT                   /note="Chaperone protein ClpB"
FT                   /id="PRO_0000191147"
FT   DOMAIN          3..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          6..71
FT                   /note="Repeat 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          83..146
FT                   /note="Repeat 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT   REGION          159..340
FT                   /note="NBD1"
FT                   /evidence="ECO:0000250"
FT   REGION          341..549
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          559..768
FT                   /note="NBD2"
FT                   /evidence="ECO:0000250"
FT   REGION          769..859
FT                   /note="C-terminal"
FT                   /evidence="ECO:0000250"
FT   COILED          391..525
FT                   /evidence="ECO:0000250"
FT   BINDING         206..213
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         609..616
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   859 AA;  95094 MW;  0E1E919D200245E2 CRC64;
     MRYDKLTAKF QQALAEAQSL ALAADSSYLE AGFVLKALLD DQNSGAAALL AHAGVNVPQV
     KQRLQQHLNS LPKVSGQGGD ILPSRELQAV LNLMDKAATK RGDAYIASEL FLLALVQQND
     AAGKILKEAG 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 VKMEKETKPE AMDKIDRRLI
     QLRMEKAHVE KEKDDASKKR LELIDEEING LQKEYADLDE IWKAEKAISD GAANIKKQID
     EVKIKIEQAK RQGDLALASK LMYEDLEHLE KQRAAAERAD TDSTKPANKL LRNNVGAEEI
     AEVVSRMTGI PVSKMMEGER DKLLKMEEVL HRRVVGQDEA VRAVSDAIRR SRSGLADPNK
     PYGSFLFLGP TGVGKTELCK ALAGFLFDSE DHLIRIDMSE YMEKHAVARL IGAPPGYVGY
     EEGGYLTEQV RRKPYSVILL DEVEKAHPDV FNILLQVLDD GRLTDGQGRT VDFKNTVIVM
     TSNIGSQHIQ QMGIQDYEAV KEVVMEDVKE HFRPEMINRI DEVVVFHGLD QANIRSIAKI
     QLKGLEKRLE KQNLRLAVSD AALDIIAKAG FDPIYGARPL KRAIQSEIEN PLAKALLAGN
     YAPESEIRVE ADGDRLKFA