ID A0A0A8HQU9_STAHY Unreviewed; 607 AA.
AC A0A0A8HQU9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415, 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 ECO:0000313|EMBL:RIO46399.1};
GN ORFNames=BUZ57_04615 {ECO:0000313|EMBL:RIO46399.1}, GLV83_07940
GN {ECO:0000313|EMBL:NJI31582.1};
OS Staphylococcus hyicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1284 {ECO:0000313|EMBL:RIO46399.1, ECO:0000313|Proteomes:UP000285625};
RN [1] {ECO:0000313|EMBL:RIO46399.1, ECO:0000313|Proteomes:UP000285625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 5959 {ECO:0000313|EMBL:RIO46399.1,
RC ECO:0000313|Proteomes:UP000285625};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
RN [2] {ECO:0000313|EMBL:NJI31582.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=1380 {ECO:0000313|EMBL:NJI31582.1};
RA Rhoads D., Shwani A., Adkins P., Calcutt M., Middleton J.;
RT "Whole genome comparisons of Staphylococcus agnetis isolates from cattle
RT and chickens.";
RL Submitted (NOV-2019) 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:RIO46399.1}.
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DR EMBL; WMFP01000037; NJI31582.1; -; Genomic_DNA.
DR EMBL; QXVO01000010; RIO46399.1; -; Genomic_DNA.
DR RefSeq; WP_039645498.1; NZ_WMFP01000037.1.
DR AlphaFoldDB; A0A0A8HQU9; -.
DR STRING; 1284.SHYC_06645; -.
DR GeneID; 41073118; -.
DR KEGG; shu:SHYC_06645; -.
DR HOGENOM; CLU_005965_2_1_9; -.
DR Proteomes; UP000285625; Unassembled WGS sequence.
DR Proteomes; UP000606275; 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; 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; 2.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 573..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..249
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 479..571
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 573..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 173
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 607 AA; 65804 MW; ADA30DB4F3516B5C CRC64;
MSKVIGIDLG TTNSCVSVLE GDEPKVIQNP EGARTTPSVV AFKNGETQVG EVAKRQAITN
PNTIQSIKRH MGTDYKENID GKSYTPQEIS AMILQNLKNT AESYLGEKVE KAVITVPAYF
NDSERQATKD AGKIAGLEVE RIINEPTAAA LAYGLDKTDK DEKVLVFDLG GGTFDVSILE
LGDGVFEVLA TAGDNRLGGD DFDQVIIDYL VKEFKSENGV DLSKDKMALQ RLKDAAEKAK
KDLSGVSSTQ ISLPFISAGE AGPLHLETTL SRAKFEELAD SLIAKTMAPT RQALSDAGLS
TSDIDEVILV GGSTRIPAVQ EAIKKEIGKE PNKGVNPDEV VAMGAAIQGG VITGDVKDVV
LLDVTPLSLG IEIMGGRMNT LIERNTTIPT SKSQVYSTAA DNQPSVDIHV LQGERPMASD
NKTLGRFQLT DIPPAPRGIP QIEVTFDIDK NGIVNVTAKD LGTNKEQKIT IESSSALSDD
EIERMVKDAE ENAEADKKRR EEVDLRNDAD QLVFQVDKML SDLGENVSED DKKEAEAKKD
DLKSALEGTD LEEIKSKKEA LEQVIQQLSM KVYEQAQQAQ SQQGQTSKQD DTVEDAEFKE
VKDDDNK
//
