ID K9S4T4_9CYAN Unreviewed; 664 AA.
AC K9S4T4;
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=GEI7407_1140 {ECO:0000313|EMBL:AFY65637.1};
OS Geitlerinema sp. PCC 7407.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC Geitlerinemataceae; Geitlerinema.
OX NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY65637.1, ECO:0000313|Proteomes:UP000010383};
RN [1] {ECO:0000313|EMBL:AFY65637.1, ECO:0000313|Proteomes:UP000010383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY65637.1,
RC ECO:0000313|Proteomes:UP000010383};
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 genome of Geitlerinema sp. PCC 7407.";
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; CP003591; AFY65637.1; -; Genomic_DNA.
DR RefSeq; WP_015171204.1; NC_019703.1.
DR AlphaFoldDB; K9S4T4; -.
DR STRING; 1173025.GEI7407_1140; -.
DR KEGG; gei:GEI7407_1140; -.
DR PATRIC; fig|1173025.3.peg.1283; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_3; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000010383; 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; 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; 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 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:UP000010383};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 614..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 664 AA; 73481 MW; 891AFC73E5BB8D26 CRC64;
MGKVVGIDLG TTNSVVAVME GGKPVVIANA EGMRTTPSVV GFSKEGERLV GQMARRQTVL
NPQNTFYGVK RFMGRKYSEL TPASKRVPYT IRRDENANIR IKCPRLERDF APEEISAMVL
RKLADEASRY LGQPVTGAVI TVPAYFNDSQ RQATRDAGRI AGLEVKRILN EPTAASLAYG
LDRANNQTIL VFDLGGGTFD VSVLEVGDGV FEVKATSGDT QLGGNDFDEK IVDWLADQFL
EAEGVDLRRD RQALQRLTEA SEKAKIELSG VNVTDINLPF ITATADGPKH LETRLTRVQF
EDLCRDLVER LRYPVKQALA DAGLSPNAID EVVLVGGSTR MPMVQDLVRS LVDLEPNQNV
NPDEVVAVGA AIQAGILGGE VKDILLLDVT PLSMGLETIG GVMKKIIPRN TTIPVRRSDI
FSTSENNQSV VEVHVLQGER DIASGNKSLG RFKLTGIPPA PRGVPQVQIS FDIDANGILQ
VMALDKTTGR EQGLTIQGAS TLSTEEVEQM IREAEEFAES DRLKKARVDK RNKAEAIALK
AERKLREVAL DFGMYFASDR RKKIEGLIRE LRECLDQEDD RGVDLAQADL QDALYELDRE
VRISIQDEEE EGFFEPLRRT FSGDRDRDRR RDDRPLYGGS SGSRSGTSTY NYDNDEWDDD
DDWL
//
