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Database: UniProt
Entry: D7DWI6_NOSA0
LinkDB: D7DWI6_NOSA0
Original site: D7DWI6_NOSA0 
ID   D7DWI6_NOSA0            Unreviewed;       622 AA.
AC   D7DWI6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000256|HAMAP-Rule:MF_00332};
DE   AltName: Full=HSP70 {ECO:0000256|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock 70 kDa protein {ECO:0000256|HAMAP-Rule:MF_00332};
DE   AltName: Full=Heat shock protein 70 {ECO:0000256|HAMAP-Rule:MF_00332};
GN   Name=dnaK {ECO:0000256|HAMAP-Rule:MF_00332};
GN   OrderedLocusNames=Aazo_2048 {ECO:0000313|EMBL:ADI64103.1};
OS   Nostoc azollae (strain 0708) (Anabaena azollae (strain 0708)).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=551115 {ECO:0000313|EMBL:ADI64103.1, ECO:0000313|Proteomes:UP000001511};
RN   [1] {ECO:0000313|EMBL:ADI64103.1, ECO:0000313|Proteomes:UP000001511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0708 {ECO:0000313|EMBL:ADI64103.1,
RC   ECO:0000313|Proteomes:UP000001511};
RX   PubMed=20628610; DOI=10.1371/journal.pone.0011486;
RA   Ran L., Larsson J., Vigil-Stenman T., Nylander J.A., Ininbergs K.,
RA   Zheng W.W., Lapidus A., Lowry S., Haselkorn R., Bergman B.;
RT   "Genome erosion in a nitrogen-fixing vertically transmitted endosymbiotic
RT   multicellular cyanobacterium.";
RL   PLoS ONE 5:E11486-E11486(2010).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC       ECO:0000256|HAMAP-Rule:MF_00332}.
CC   -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000256|HAMAP-
CC       Rule:MF_00332}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00332,
CC       ECO:0000256|RuleBase:RU003322}.
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DR   EMBL; CP002059; ADI64103.1; -; Genomic_DNA.
DR   RefSeq; WP_013191120.1; NC_014248.1.
DR   AlphaFoldDB; D7DWI6; -.
DR   STRING; 551115.Aazo_2048; -.
DR   KEGG; naz:Aazo_2048; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_3; -.
DR   OrthoDB; 5410377at2; -.
DR   Proteomes; UP000001511; 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   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
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   NCBIfam; TIGR02350; prok_dnaK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR   PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00332}; Chaperone {ECO:0000256|HAMAP-Rule:MF_00332};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00332};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_00332}; Reference proteome {ECO:0000313|Proteomes:UP000001511};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          600..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          247..274
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   622 AA;  67483 MW;  B60FBF94E9C6204C CRC64;
     MAKVVGIDLG TTNSCVAVME GGQPLVIANS EGQRITPSVV AYTKTGERLV GQIARRQAVM
     NPENTFYSVK RFIGRKYEEI THEATEVSYR TLRDSNANVK LNCPAAGQEF APEEISAQVL
     RKLVDDASKY LGEKVTQAVI TVPAYFNDSQ RQATKDAGKI AGLDVLRIIN EPTAAALAYG
     LDKKENETIL VFDLGGGTFD VSILEVGDGV FEVKSTSGDT HLGGDDFDKK IVDWLANQFQ
     SNEGIDLRKD KQALQRLTEA AEKAKIELSS ATQTNINLPF ITATQAGPKH LDMMLTRGKF
     EEMTADLLDR CRKPVQQALQ DAKLSNAQLD EIVLVGGSTR IPAVQELVRR MTGKEPCQGV
     NPDEVVAVGA AIQAGVLSGE VKDILLLDVT PLSLGVETIG GVMTKIISRN TTIPVKKSEV
     FSTAADGQSN VEVHVLQGER ELAKDNKSLG TFRLDGIPPA PRGVPQIDVT FDIDANGILS
     VTAKDKATGK QQSISITGAS TLDKRDVEKM VRDAESHAEE DRRRREQIDT KNLGDSLVYQ
     AEKQLRDLGD KVSAVDRGRV EDLVKDLAEA INQDHFDRIK SLSSQLQQVL MQVGSTVYAQ
     AGSSDGSSRS EDVIDADFVE NK
//
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