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Database: UniProt
Entry: B2J1R4_NOSP7
LinkDB: B2J1R4_NOSP7
Original site: B2J1R4_NOSP7 
ID   B2J1R4_NOSP7            Unreviewed;       879 AA.
AC   B2J1R4;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 107.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   OrderedLocusNames=Npun_F3510 {ECO:0000313|EMBL:ACC81916.1};
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC81916.1, ECO:0000313|Proteomes:UP000001191};
RN   [1] {ECO:0000313|Proteomes:UP000001191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA   Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACC81916.1, ECO:0000313|Proteomes:UP000001191}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191};
RX   PubMed=23463784; DOI=10.1104/pp.112.213116;
RA   Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT   "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT   Cyanobacterium-Plant Symbiosis.";
RL   Plant Physiol. 161:1984-1992(2013).
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. {ECO:0000256|RuleBase:RU362034}.
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|ARBA:ARBA00004496,
CC       ECO:0000256|RuleBase:RU362034}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP001037; ACC81916.1; -; Genomic_DNA.
DR   RefSeq; WP_012409890.1; NC_010628.1.
DR   AlphaFoldDB; B2J1R4; -.
DR   STRING; 63737.Npun_F3510; -.
DR   EnsemblBacteria; ACC81916; ACC81916; Npun_F3510.
DR   KEGG; npu:Npun_F3510; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_3; -.
DR   OMA; GPEHILM; -.
DR   OrthoDB; 438311at2; -.
DR   PhylomeDB; B2J1R4; -.
DR   Proteomes; UP000001191; Chromosome.
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:UP000001191};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT   DOMAIN          6..148
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   COILED          439..531
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   879 AA;  99014 MW;  F0401088E3051E8E CRC64;
     MQPTDPNKFT DKAWEAIVKS QDIVRAYQQQ QLDVEHLIIA LLEEPTSLAI RILARSEVDP
     IRFQQQLEAF IQRQPKVGKS DQLYLSRSLD VLLDKAEEAR VRMKDSYISV EHILLAFAED
     DRIGRKILKS FSADAAKLEA TIKAVRGSQK VTDQSPESRY EALQKFGRDL TEQAKAGKLD
     PVIGRDDEIR RVIQVLSRRS KNNPVLIGEP GVGKTAIAEA LAQRMVNGDV PESLKNRQLI
     SLDIGSLIAG AKLRGEFEER LKAVLKEVMD SNGQIVLFID ELHTVVGTGS SQQGAMDAGN
     LLKPMLARGE LRCIGATTLD EFRKHIEKDA ALERRFQQVF VDQPSVENTI SILRGLKERY
     EVHHNVKISD SALVAAATLS ARYISDRFLP DKAIDLVDEA AAQLKMEITS KPAELETIDR
     RLMQLEMEKL SLAGEEKGTP QTKERLERIE QEIANLTEKQ QIFNEQWQGE KQILEAISAL
     KKEEDALRVQ IEQAERAYDL NKAAQLKYGK LEGVQHEREA KEASLLEIQN QGSTLLREQV
     TEADIAEIVA KWTGIPVNRL LESERQKLLQ LESHLHQRVI GQEEAVEAVA AAIRRARAGM
     KDPSRPIGSF LFMGPTGVGK TELARALAQF LFDSDDALVR LDMSEYMEKH SVSRLVGAPP
     GYVGYEEGGQ LSEAVRRRPY SVVLLDEVEK AHPDVFNILL QVLDDGRITD SQGRTVDFRN
     SVIVMTSNIG SEHILDVSGD SQYETMRKRV MEGLRSHFRP EFLNRVDDII LFHTLNRTEM
     RQIIRIQLKR VENLLREQKI FFEISQAACD HLVESGYDPV YGARPLKRAI QREVENPLAT
     KLLENTFISG DTILIDKNEN GLSFSKKVLV KVSVPQIAT
//
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