ID A0A1Q8ZCN9_9CYAN Unreviewed; 738 AA.
AC A0A1Q8ZCN9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BST81_13620 {ECO:0000313|EMBL:OLP18061.1};
OS Leptolyngbya sp. 'hensonii'.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC Leptolyngbya group; Leptolyngbya.
OX NCBI_TaxID=1922337 {ECO:0000313|EMBL:OLP18061.1, ECO:0000313|Proteomes:UP000186296};
RN [1] {ECO:0000313|EMBL:OLP18061.1, ECO:0000313|Proteomes:UP000186296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=hensonii {ECO:0000313|Proteomes:UP000186296};
RA Hamilton T.L., Klatt J.M., De Beer D., Macalady J.;
RT "Physiology of photosynthesis in the novel isolate Oscillatoriales
RT cyanobacterium hensonii.";
RL Submitted (NOV-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLP18061.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MQTZ01000041; OLP18061.1; -; Genomic_DNA.
DR RefSeq; WP_075599021.1; NZ_MQTZ01000041.1.
DR AlphaFoldDB; A0A1Q8ZCN9; -.
DR STRING; 1922337.BST81_13620; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000186296; Unassembled WGS sequence.
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:UP000186296};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 647..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..711
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 738 AA; 83187 MW; 5D9FA1DF5B69BA73 CRC64;
MGKVVGIDLG TTNSVVAVME GGKPVVIANA EGVRTTPSVV GFSKDGERLV GQMARRQTVL
NPQNTFYGVK RYIGRKYSEL SPESKRVPYT IRKDEVGNIK IKCPRLDKEF APEEISAMVL
RKLVDDASRY LGEKVTRAVI TVPAYFNDSQ RQATRDAGRI AGLDVLRILN EPTAASLAYG
LEKRDQQTIL VFDLGGGTFD VSILDVGDGV FEVKATSGDT QLGGTDFDRR IVDWLAEQFL
EAEGVDLRRD RQSLQRLTEA AEKAKIELSG VTITDINLPF ITATEDGPKH LETRLARTQF
EELCGDLLDR LRGPVKRALS DADLTAADID EVVLVGGSTR IPAVQKLVRK IINLEPNQNV
NPDEVVAVGA AVQAGIMAGE VKDILLLDVT PLSLGLETIG GVTRKLIPRN TTIPVRRSDI
FSTSENNQTV VEVHVVQGER EMAANNKSLG RFKLTGVPPA PRGVAQILVS FDIDANGILQ
VMALDRTTGR EQSITVQEAS TLTEEEIKKM LREAEEFADQ DREKRERIEK RTLAEDLIRQ
AEKLLRDVAM DYGMYFASDL RRRIETLLRE LRDSLDNNDE RGIDVTQVDL RDAVYDLRRE
YYRRDQDDEE DEGILGSIRR IFKGDDDEEY EYDSWNRDRR DYRDDYRNED YRNDNYRSGG
YRNDDYRNED YRSDRIRGSR SGGSRNEEYR SDRAGGYRND ANARDEESRR PAYGGGTSSR
PGRYSQNDDF DEDDDEWL
//
