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Database: UniProt
Entry: A0A0C2QWZ3_9CYAN
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ID   A0A0C2QWZ3_9CYAN        Unreviewed;       889 AA.
AC   A0A0C2QWZ3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN   Name=clpB {ECO:0000256|RuleBase:RU362034};
GN   ORFNames=SD80_14585 {ECO:0000313|EMBL:KIJ82895.1};
OS   Scytonema tolypothrichoides VB-61278.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ82895.1};
RN   [1] {ECO:0000313|EMBL:KIJ82895.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ82895.1};
RA   Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.;
RT   "Draft genome sequence of Scytonema tolypothrichoides VB-61278.";
RL   Submitted (JAN-2015) 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. {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:KIJ82895.1}.
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DR   EMBL; JXCA01000010; KIJ82895.1; -; Genomic_DNA.
DR   STRING; 1233231.SD80_14585; -.
DR   OrthoDB; 438311at2; -.
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}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Stress response {ECO:0000256|RuleBase:RU362034}.
FT   COILED          415..500
FT                   /evidence="ECO:0000256|RuleBase:RU362034"
SQ   SEQUENCE   889 AA;  100185 MW;  D83C4B2362FF248E CRC64;
     MQPTDPNKFT DKAWEAIVKS QDVVRAYQQQ QLDVEHLLIA LLEEPTGLAT RILGRCEIDA
     SRLQQQVEGF TQRQPKVGKA DQLYLSRSLD TLLDRAEEAR ARMKDSYISI EHLLLAFAED
     ERIGRRIFKS FNLDTAKLEA AIKTVRGSQK VTDQNPESRY EALQKFGRDL TEQAKSGKLD
     PVIGRDDEIR RLIQVLSRRS KNNPVLIGEP GVGKTAIAEA LAQRIINGDV PESLKNRQLI
     ALDIGSLIAG AKYRGEFEDR LKSVLKEVIE SNGQIVLFID ELHTVVGTGS TQQGAMDAGN
     LLKPMLARGE LRCIGATTLD EYRKYIEKDA ALERRFQQVF VDQPSVENTI SILRGLKERY
     EVHHNVKISD SALVAAATLS ARYISDRFLP DKAIDLVDEA AAQLKMEITS KPTELENIDR
     RLMQLEMEKL SLAGEEKATV QTKERLARIE QEIVNLTEKQ QELNGQWQGE KQLLEAISAL
     KQEEEKLRLQ IEQAERAYDL NKAAQLKYGK LEGVQRDREA KEAQLLKIQS TGTTLLREQV
     TEADIAEIVA KWTGIPVNRL LESERQKLLQ LESHLHQRVV GQQEAVSAVS AAIRRARAGM
     KDPSRPIGSF LFMGPTGVGK TELARALAQF LFDSDDALVR LDMSEYMEKH SVSRLVGAPP
     GYVGYEEGGQ LSEAIRRRPY SVVLLDEVEK AHPDVFNILL QVLDDGRITD SQGRTVDFRN
     TVIVMTSNIG SEHILDISGD DANYEKMRNR VMDALRSHFR PEFLNRVDDT ILFHTLSRSE
     MRHIIRIQLK RVENLLQEQK ISLEISSAAC DYLVETGYDP VYGARPIKRA LQREIENPVA
     TKLLENTFVP GDTIVIDKAD HGLTFNKKMV VKVPAVQNKT LLIEASREV
//
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