ID K9SKY1_9CYAN Unreviewed; 660 AA.
AC K9SKY1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 ORFNames=Pse7367_2510 {ECO:0000313|EMBL:AFY70770.1};
OS Pseudanabaena sp. PCC 7367.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY70770.1, ECO:0000313|Proteomes:UP000010386};
RN [1] {ECO:0000313|EMBL:AFY70770.1, ECO:0000313|Proteomes:UP000010386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY70770.1,
RC ECO:0000313|Proteomes:UP000010386};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003592; AFY70770.1; -; Genomic_DNA.
DR RefSeq; WP_015165726.1; NC_019701.1.
DR AlphaFoldDB; K9SKY1; -.
DR STRING; 82654.Pse7367_2510; -.
DR KEGG; pseu:Pse7367_2510; -.
DR PATRIC; fig|82654.3.peg.2935; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_3; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000010386; 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:UP000010386};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 630..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 244..271
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 660 AA; 73713 MW; 9E57B9829B5ACAB6 CRC64;
MGKIVGIDLG TTNSVVAVME AGKPIAIANA EGSRTTPSVV SFSKDGDRLI GQMARRQAVL
NPENTFYSAK RFIGRKYSEL NQDAKRVAYT VFRDQTGNIR MKCPRLSKDF APEELSAMVI
RKLVDEASRY LGEEVTGAVI TVPAYFNDSQ RQATKDAGRI AGIEVKRILN EPTAASLAYG
LDKNESQRIL VFDLGGGTFD VSILEVGDGV FEVLGTAGDT QLGGDDFDRK IVNWLAEQFK
ELEGVDLRRE RQALQRLMEA AEKAKVELST VGATSINLPF ITATADGPLH MDIDLKRSQF
ERLCEDLIER LKAPIEQVLR DSGLSTREID EVVLVGGSTR MPAVQELVRS YINKEPNQSV
NPDEVVAVGA AVQAGILTGD LKDMLLLDVT PLSLGVETYG GIFKKLITRN TTIPTRKTDL
FTTAEDNQTS VEIHVLQGEG DLAKRNKSLG RFKLSGISPQ SKGMAQVDVM FDLNADGILS
VTATDRRTGV ERRVTIKGAS TLDEREVERM VSEAEKYAEQ DRSRKERIEK INRAENLITS
SKRLLKELSL EFGYLLSYER RKDVDKLIQT LEKAIAQEDD ARIDTAQLEL QDAISTLSRE
IYEQAEYEDD YYEGDFIDDI IDRIGNFASS RSDRRPKDDY DYQRRPDTRV NWDENDDEWV
//
