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
//