DNAK2_SYNY3
ID DNAK2_SYNY3 Reviewed; 636 AA.
AC P22358;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Chaperone protein DnaK2;
DE AltName: Full=HSP70-2;
DE AltName: Full=Heat shock 70 kDa protein 2;
DE AltName: Full=Heat shock protein 70-2;
GN Name=dnaK2; Synonyms=dnaK {ECO:0000303|PubMed:1670771};
GN OrderedLocusNames=sll0170;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION BY STRESS.
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=1670771; DOI=10.1016/s0021-9258(18)52401-7;
RA Chitnis P.R., Nelson N.;
RT "Molecular cloning of the genes encoding two chaperone proteins of the
RT cyanobacterium Synechocystis sp. PCC 6803.";
RL J. Biol. Chem. 266:58-65(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA Sugiura M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT from map positions 64% to 92% of the genome.";
RL DNA Res. 2:153-166(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
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).
RN [4]
RP INDUCTION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=15471853; DOI=10.1074/jbc.m410162200;
RA Paithoonrangsarid K., Shoumskaya M.A., Kanesaki Y., Satoh S., Tabata S.,
RA Los D.A., Zinchenko V.V., Hayashi H., Tanticharoen M., Suzuki I.,
RA Murata N.;
RT "Five histidine kinases perceive osmotic stress and regulate distinct sets
RT of genes in Synechocystis.";
RL J. Biol. Chem. 279:53078-53086(2004).
RN [5]
RP INDUCTION.
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=15805106; DOI=10.1074/jbc.m412174200;
RA Shoumskaya M.A., Paithoonrangsarid K., Kanesaki Y., Los D.A.,
RA Zinchenko V.V., Tanticharoen M., Suzuki I., Murata N.;
RT "Identical Hik-Rre systems are involved in perception and transduction of
RT salt signals and hyperosmotic signals but regulate the expression of
RT individual genes to different extents in synechocystis.";
RL J. Biol. Chem. 280:21531-21538(2005).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC -!- INDUCTION: By stress conditions; heat shock, ultraviolet and oxidative
CC stress (PubMed:1670771). Induced by hyperosmotic stress (0.5 M
CC sorbitol) under control of hik34 and rre1 (PubMed:15471853). Induced by
CC salt stress (0.5 M NaCl) under control of hik34 and rre1
CC (PubMed:15805106). {ECO:0000269|PubMed:15471853,
CC ECO:0000269|PubMed:15805106, ECO:0000269|PubMed:1670771}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; M57518; AAA27287.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA10059.1; -; Genomic_DNA.
DR PIR; C39025; C39025.
DR AlphaFoldDB; P22358; -.
DR SMR; P22358; -.
DR IntAct; P22358; 1.
DR STRING; 1148.1001435; -.
DR PaxDb; P22358; -.
DR PRIDE; P22358; -.
DR EnsemblBacteria; BAA10059; BAA10059; BAA10059.
DR KEGG; syn:sll0170; -.
DR eggNOG; COG0443; Bacteria.
DR InParanoid; P22358; -.
DR OMA; AYTKNQD; -.
DR PhylomeDB; P22358; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..636
FT /note="Chaperone protein DnaK2"
FT /id="PRO_0000078569"
FT REGION 604..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
SQ SEQUENCE 636 AA; 67614 MW; 33AE4CECBA28F40A CRC64;
MGKVVGIDLG TTNSCVAVME GGKPTVIANA EGFRTTPSVV GYAKNGDRLV GQIAKRQAVM
NPGNTFYSVK RFIGRKFDEI TNEATEVAYS VVKDGNGNVK LDCPAQGKQF APEEISAQVL
RKLVDDASKY LGETVTQAVI TVPAYFNDSQ RQATKDAGKI AGIEVLRIIN EPTAASLAYG
LDKKDNETIL VFDLGGGTFD VSILEVGEGV FEVLATSGDT HLGGDDFDKK IVDFLAGEFQ
KAEGIDLRKD KQALQRLTEA AEKAKIELSG VSQTEINLPF ITATQDGPKH LDTTLSRAKF
EEICSDLIDR CGIPVENAIR DAKIDKSALD EIVLVGGSTR IPAVQEVVKK ILGKDPNQGV
NPDEVVAVGA AIQGGVLSGE VKDILLLDVS PLSLGVETLG GVMTKIIPRN TTIPTKKSET
FSTAVDGQSN VEIHVLQGER EMANDNKSLG TFRLDGIPPA PRGVPQIEVT FDIDANGILN
VTAKDRGTGK EQSISITGAS TLPDTEVDRM VKEAESNAAA DKERREKIDR KNQADSLVYQ
AEKQITELGD KVPAADKIKA EGLIKDLKEA VAQEDDAKIQ TVMPELQQVL YSIGSNMYQQ
AGAEAGVGAP GAGPEAGTSS GGGDDVIDAE FSEPEK
