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Database: UniProt
Entry: A0A0N8KNK0_9CYAN
LinkDB: A0A0N8KNK0_9CYAN
Original site: A0A0N8KNK0_9CYAN 
ID   A0A0N8KNK0_9CYAN        Unreviewed;       657 AA.
AC   A0A0N8KNK0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:KPQ36754.1};
GN   Name=htpG {ECO:0000313|EMBL:KPQ36754.1};
GN   ORFNames=HLUCCA11_04510 {ECO:0000313|EMBL:KPQ36754.1};
OS   Phormidesmis priestleyi Ana.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Phormidesmis.
OX   NCBI_TaxID=1666911 {ECO:0000313|EMBL:KPQ36754.1, ECO:0000313|Proteomes:UP000050465};
RN   [1] {ECO:0000313|EMBL:KPQ36754.1, ECO:0000313|Proteomes:UP000050465}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ana {ECO:0000313|EMBL:KPQ36754.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC       {ECO:0000256|ARBA:ARBA00008239}.
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:KPQ36754.1}.
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DR   EMBL; LJZR01000004; KPQ36754.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N8KNK0; -.
DR   STRING; 1666911.HLUCCA11_04510; -.
DR   PATRIC; fig|1666911.3.peg.2905; -.
DR   Proteomes; UP000050465; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd16927; HATPase_Hsp90-like; 1.
DR   Gene3D; 3.30.230.80; -; 1.
DR   Gene3D; 3.40.50.11260; -; 1.
DR   Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR037196; HSP90_C.
DR   InterPro; IPR001404; Hsp90_fam.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   PANTHER; PTHR11528:SF97; ENDOPLASMIN; 1.
DR   PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR   Pfam; PF13589; HATPase_c_3; 1.
DR   Pfam; PF00183; HSP90; 2.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ   SEQUENCE   657 AA;  74855 MW;  65037A252FCD3EE5 CRC64;
     MTATVLEKGN ISIHTENIFP IIKKWLYSDH EIFIRELVSN GVDAISKLSM ISRSGEYQGE
     VTSEITIAID KEAKTLSITD SGIGMTADEI KKYINQVAFS SAEEFITKFK DNDDQQIIGH
     FGLGFYSSFM VADRVDIDTL SWQEGAEAVH WSCDGSTSFE LSQSDRTTRG TTVTLHLNDD
     EQEYLEEARI KQLVKTYCDF MPVPIKLGDD AINKQEALWK KSPSDLTDED YLNLYRYLYP
     FEEEPLLWVH LNTDYPFVVN GILYFPKLKP DVELNKGQIK LFCNQVFVSD NCEEIIPKFL
     TPLRGVIDST DIPLNVSRSF LQADRTVKRI ADYVAKKVGD RLKELYRDDL SEYVRIWQDL
     GTFAKFGSLN DDKFKKQIQD YVIFRSTSDL AKSDEPTVEV QTEESDEWAD VNKKSAVDAN
     GASYTTIKEY LERNKEKHEN RIYYATDEVS QSTYISLLKN QDLEVLFMDS FIDTHFVSFL
     EQEYSDVKFS RVDADLDDTL IDSDKEAEIV DATTNKTRSE QIKDVFTKSL NRPQITIRTE
     ALKSVDQSAP PAMVLVPEEL RRMQEMSAFL QQQGVQFPES HTLLVNTAHP LIQNLAKLDQ
     GSIVQPDGSP SPAEQLASLI CEQVYDLALM AQKGFDADGM KAFTERSTNL LTKLTER
//
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