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
//