ID K9WAH4_9CYAN Unreviewed; 656 AA.
AC K9WAH4;
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=Mic7113_0867 {ECO:0000313|EMBL:AFZ16769.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ16769.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ16769.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ16769.1,
RC ECO:0000313|Proteomes:UP000010471};
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., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-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; CP003630; AFZ16769.1; -; Genomic_DNA.
DR RefSeq; WP_015180929.1; NC_019738.1.
DR AlphaFoldDB; K9WAH4; -.
DR STRING; 1173027.Mic7113_0867; -.
DR KEGG; mic:Mic7113_0867; -.
DR PATRIC; fig|1173027.3.peg.954; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_3; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000010471; 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:UP000010471};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 605..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 553..591
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 605..637
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 656 AA; 71432 MW; 5BD7AC0B64F9BB63 CRC64;
MGKVIGIDLG TTNSCVAVLE GGQPIVISST EGGRTTPSIV GFGKAGERLV GQLAKRQAVT
NAENTIYSIK RFIGRRWDDT ATERSRVPYN CVKGRDDTVD VQIRGRTYTP QEISAMILQK
LKADAESFLG ESVEQAVITV PAYFTDAQRQ ATKDAGTIAG LEVLRIINEP TAASLAYGLD
KQSEEQRILV FDLGGGTFDV SILQLGDGVF EVKATSGNNH LGGDDFDNVI VRWMIENFKG
TEGIDLGTDK MALQRLREAA EKAKVELSSM LSTSINLPFI TADETGPKHL EMELSRSKFE
ELASELITGT IEPVTQSLKD ADLKPDDIDR ILLVGGSTRI PAVQEAIKKF FGGRTPDKSV
NPDEAVALGA AIQGGVLGGE VEDLLLLDVT PLSLGIETLG EVFTKIIDRN TTIPTSKSQV
FSTATDGQTS VEIHVLQGER AMARDNKSLG KFLLTGIPPA PRGVPQIEVS FEIDVNGILQ
VSAADKGTGK EQRIRITNTG GLSASEVERM RVEAEKYAED DRRRIQLVEL KNQADSLFYS
YEGTLKESGD LVREDLKAQG EEKKQQLQQA MADSSISIEE VKQRLEDFQQ KLFEIGAAVY
QQASPSVDTD EFVQTEEVSS TPEFSQPFES PSTSEEDDLI LNFDEETVTA DYEAVD
//
