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Database: UniProt
Entry: A0A139X452_9CYAN
LinkDB: A0A139X452_9CYAN
Original site: A0A139X452_9CYAN 
ID   A0A139X452_9CYAN        Unreviewed;       889 AA.
AC   A0A139X452;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=WA1_32260 {ECO:0000313|EMBL:KYC39402.1};
OS   Scytonema hofmannii PCC 7110.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC39402.1, ECO:0000313|Proteomes:UP000076925};
RN   [1] {ECO:0000313|EMBL:KYC39402.1, ECO:0000313|Proteomes:UP000076925}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC39402.1,
RC   ECO:0000313|Proteomes:UP000076925};
RX   PubMed=23221676; DOI=10.1093/gbe/evs117;
RA   Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA   Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA   Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT   "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT   of oxygenic photosynthesis from prokaryotes to plastids.";
RL   Genome Biol. Evol. 5:31-44(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}.
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:KYC39402.1}.
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DR   EMBL; ANNX02000035; KYC39402.1; -; Genomic_DNA.
DR   RefSeq; WP_017747386.1; NZ_KQ976354.1.
DR   AlphaFoldDB; A0A139X452; -.
DR   STRING; 128403.WA1_32260; -.
DR   OrthoDB; 438311at2; -.
DR   Proteomes; UP000076925; 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:UP000076925};
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..500
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   889 AA;  100117 MW;  12DD7B0C7BE574E0 CRC64;
     MQPTDPNKFT DKAWEAIVKS QDIVRAYQQQ QLDVEHLVLA LLEEPTGLAT RIFSRCEIDP
     SRLQQQLEAF TQRQAKVGKN DQLYLGRSLD LMLDKAEEAR ARMKDGFISI EHLLLAFTED
     DRIGRRVLKS FNVDAVKLEA TIRSVRGSQK VTDQNPESRY EALQKFGRDL TEQAKAGKLD
     PVIGRDDEIR RVVQVLSRRS KNNPVLIGEP GVGKTAIAEA LAQRIVNGDV PESLKNRQLM
     ALDIGSLIAG AKYRGEFEDR LKSVLREVTE SNGQIVLFID ELHTVVGTGS NQQGSMDAGN
     LLKPMLARGE LRCIGATTLD EYRKFIEKDA ALERRFQQVF VDQPSVEDTI SILRGLKERY
     EVHHNVKISD SALVAAATLS ARYISDRFLP DKAIDLVDEA AAQLKMEITS KPTELEIIDR
     RLMQLEMEKL SLAGEEKATV QTKERFERIE QEITNLTEKQ QNLNNQWQGE KQLLEAISAL
     KQEEEKLRVQ IEQAERAYDL NKAAQLKYGK LEGVQRDRET KETQLLEIQS TGATLLREQV
     TESDIAEIVA KWTGIPVNSL LESERKKLLQ LENHLHERVV GQQEAVSAVA AAIRRARAGM
     KDPSRPIGSF LFMGPTGVGK TELARALAKF LFDSADALVR LDMSEYMEKH SVSRLVGAPP
     GYVGYEEGGQ LSEAVRRRPY SVVLLDEVEK AHPDVFNILL QVLDDGRITD SQGRTVDFRN
     AVIVMTSNIG SEHILDISGD DANYEKMRNR VMDALRSHFR PEFLNRVDDI ILFHTLNRSE
     MRKIVRIQLK RVESLLNEQK ISLEISAAAC DRLVEVGYDP VYGARPIKRA IQREVENPLA
     TKLLENTFVP GDTVVIDVGD NELMFSKKMV VKVPATQGKT LLIEASREA
//
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