ID A5GTR5_SYNR3 Unreviewed; 634 AA.
AC A5GTR5;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Chaperone protein htpG {ECO:0000313|EMBL:CAK28274.1};
GN Name=htpG {ECO:0000313|EMBL:CAK28274.1};
GN OrderedLocusNames=SynRCC307_1371 {ECO:0000313|EMBL:CAK28274.1};
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK28274.1, ECO:0000313|Proteomes:UP000001115};
RN [1] {ECO:0000313|Proteomes:UP000001115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; CT978603; CAK28274.1; -; Genomic_DNA.
DR AlphaFoldDB; A5GTR5; -.
DR STRING; 316278.SynRCC307_1371; -.
DR KEGG; syr:SynRCC307_1371; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_2_3; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000001115; Chromosome.
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; IPR003594; HATPase_C.
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; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001115}.
FT DOMAIN 27..178
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 634 AA; 70770 MW; 520AF0D20079BCEA CRC64;
MSVLEQGQIQ IHTENIFPII KKAVYSGHEV FLRELVSNGT DAISKRRMAA MAGDCSEGSD
GLISIKIDRE AKTLTISDNG IGMNADEVKR YINQVAFSSA EEFLEKYKSE DDAIIGHFGL
GFYSSFMVAS QVELVSLSAR PNAEAVRWSC DGSPNFSLEA AERSEPGTDV ILHLQEEELE
YIEPARIRTL INTYCDFMPV EVQLEGETVN KREAPWRKSP RELSDEDYIE LYRYLYPFQG
DPLLWVHLNT DYPYNLQGIL YFPKSTGRAD WEKGEIKLYC NQVFVSDSIK EVVPKYLLPL
RGVIDSPDIP LNVSRSALQT DRRVRSIGGF VAKKVGDRLK QLHRDEPKRY AEIWESLAPF
IKIGAMEDEK FADQVAELVL FGTTAAAGEG ETPDPVAAED GKRFTTLGGY RSRLSADNDK
RILYCTDEAG QAGALALWQG QGAEVLLADT FIDTQFIPWL EYRHEELKFQ RVDAELDDSL
QDKDSGVTDA EGKDSSESLR DLFKASLDND KVTIQVQALK GDNAPAALIL LPEQMRRMND
MGALMEQRLP GLPDHHVLLI NRRHRLVEGM QKLAAGSVIA GGGASSPSQQ LAEQLSRHVY
EMAKLSVGGL EPNELAGFQQ RSCDLMGELM NRGL
//
