ID A0A1U9RFB3_9GAMM Unreviewed; 644 AA.
AC A0A1U9RFB3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=B2G49_20825 {ECO:0000313|EMBL:AQU84819.1};
OS Halomonas sp. 'Soap Lake #7'.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1962264 {ECO:0000313|EMBL:AQU84819.1, ECO:0000313|Proteomes:UP000189672};
RN [1] {ECO:0000313|EMBL:AQU84819.1, ECO:0000313|Proteomes:UP000189672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soap Lake #7 {ECO:0000313|EMBL:AQU84819.1,
RC ECO:0000313|Proteomes:UP000189672};
RA Peterson S.W.;
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AQU84819.1, ECO:0000313|Proteomes:UP000189672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soap Lake #7 {ECO:0000313|EMBL:AQU84819.1,
RC ECO:0000313|Proteomes:UP000189672};
RA Mormile M.R.;
RT "Halomonas from Soap Lake, Washington USA.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {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; CP019915; AQU84819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9RFB3; -.
DR STRING; 1962264.B2G49_20825; -.
DR KEGG; haso:B2G49_20825; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000189672; 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 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:SF541; CHAPERONE PROTEIN DNAK; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
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 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 605..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 644 AA; 69318 MW; 8D8A4FE6A3E8DD53 CRC64;
MGRIIGIDLG TTNSCVAVLD GDSAKVIENA EGGRTTPSII AYTDDGETLV GQAAKRQAVT
NPENTLYAIK RLIGRRFKDD VVQKDIKMVP YKIAEADNGD AWVEVKGKRM APPQVSAEVL
KKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAYG
MDKSRGDKTI AVYDLGGGTF DISIIEVADV DGETQFEVLA TNGDTFLGGE DFDLALINYL
VDQFKADSGI DLSGDNLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADN TGPKHLNVKV
TRAKLESLVE ELVQRSLEPC KMALKDAGLS ASEIDEVILV GGQTRMPMVQ KKAADFFGKE
ARKDVNADEA VAVGAAIQGG VLGGDVKDVL LLDVTPLTLG IETMGGVMTA LIDKNTTIPT
KKTQTFSTAD DNQTAVTIHV VQGERKQVSQ NKSLGRFDLA EIPPAPRGVP QIEVAFDLDA
NGILNVSAKD KATNKVQSIV IKASSGLTDE EIEQMVRDAE AHADEDKKFE ALVQLRNQAD
GMIHATRKTV QEAGDKATDD EKQAIETAIT ELEEAIKTDD QDNIQKKLDA LTEASGQLAQ
KMYAEQAEAA QQAEGDGAES ANAKQDDDVV DAEYEEVNDD KKQQ
//
