ID Q55807_SYNY3 Unreviewed; 531 AA.
AC Q55807;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE SubName: Full=Slr0086 protein {ECO:0000313|EMBL:BAA10560.1};
GN OrderedLocusNames=slr0086 {ECO:0000313|EMBL:BAA10560.1};
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae;
OC Synechocystis.
OX NCBI_TaxID=1111708 {ECO:0000313|EMBL:BAA10560.1, ECO:0000313|Proteomes:UP000001425};
RN [1] {ECO:0000313|EMBL:BAA10560.1, ECO:0000313|Proteomes:UP000001425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa {ECO:0000313|Proteomes:UP000001425};
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|RuleBase:RU003322}.
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DR EMBL; BA000022; BAA10560.1; -; Genomic_DNA.
DR PIR; S76616; S76616.
DR AlphaFoldDB; Q55807; -.
DR STRING; 1148.gene:10500064; -.
DR PaxDb; 1148-1001723; -.
DR EnsemblBacteria; BAA10560; BAA10560; BAA10560.
DR KEGG; syn:slr0086; -.
DR eggNOG; COG0443; Bacteria.
DR InParanoid; Q55807; -.
DR PhylomeDB; Q55807; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd10170; HSP70_NBD; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF513; SLR0086 PROTEIN; 1.
DR Pfam; PF00012; HSP70; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000001425}.
SQ SEQUENCE 531 AA; 59185 MW; 254FD53C7267A13B CRC64;
MPYAIDFGTT NTVIARWNEA TRQGNLIDLP SLSHPLGDSG PLVPSLLYVE NAALGQVAIA
REVLDRGRDI STDTRFFKNF KRGIGVAVQG FLPQLDGHTL SLETLGQWYL DKLIRILTEQ
EGQGPDCLAL TVPVDSFESY RHWLSHTCRS WGVEEVRLVD EPTAAALGYG VGDASQILVL
DFGGGTVDFS WVQLGDRGQK GRSGFLLKWG GILGGSKAEE KSALAKVLAK AGANLGGSDI
DYWISEYFTE AQGLQVSPWI RRLAERLKIA LGEAEEATEV YFDDQALESY EFQLRRSDLT
EILQQRQFFE RLTALWEQVQ QTAQRRGLTP ANLDAVLVVG GTSQLPMVQD WINAQFPAGK
IRNQQPFGAI ALGALQIYQG REVQDYLYHS YGVRYWNRRK NSHNWHPIIK NGQTYPMAEP
IELTLGASLD NQPSIELIVG ELGSSIGATE VYFDGNQLIT RVLENQAFTV QPLNDRNGAR
QIAQLSPPGV PGGDRIKVKF WVDDQRYLRL TVEDLLQQKL LLENQVVAQL R
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