ID A0A0F7M9P7_9GAMM Unreviewed; 640 AA.
AC A0A0F7M9P7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=IMCC21906_03138 {ECO:0000313|EMBL:AKH70777.1};
OS Spongiibacter sp. IMCC21906.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae; Spongiibacter.
OX NCBI_TaxID=1620392 {ECO:0000313|EMBL:AKH70777.1, ECO:0000313|Proteomes:UP000035013};
RN [1] {ECO:0000313|EMBL:AKH70777.1, ECO:0000313|Proteomes:UP000035013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC21906 {ECO:0000313|EMBL:AKH70777.1,
RC ECO:0000313|Proteomes:UP000035013};
RA Cho J.-C., Yang S.-J., Kang I.;
RT "Complete genome sequence of IMCC21906 belonging to the
RT Gammaproteobacteria.";
RL Submitted (MAY-2015) 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; CP011477; AKH70777.1; -; Genomic_DNA.
DR RefSeq; WP_047012914.1; NZ_CP011477.1.
DR AlphaFoldDB; A0A0F7M9P7; -.
DR STRING; 1620392.IMCC21906_03138; -.
DR KEGG; spoi:IMCC21906_03138; -.
DR PATRIC; fig|1620392.3.peg.3247; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000035013; 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}; Reference proteome {ECO:0000313|Proteomes:UP000035013};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 605..640
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 640 AA; 68736 MW; 762FE5E4F77E5971 CRC64;
MAKIIGIDLG TTNSCVAVMD GDKVKVIENA EGTRTTPSIV AYTDDNEILV GQSAKRQAVT
NPNNTLYAVK RLIGRRFEDD VVQKDIKMVP YGICKADNGD AWVEVKGEKM APPQISAEVL
KKMKKTAEDY LGEKVTEAVI TVPAYFNDSQ RQATKDAGRI AGLEVKRIIN EPTAAALAYG
MDKAKGDRTV AVYDLGGGTF DISIIEIAEV DGEHQFEVLS TNGDTFLGGE DFDMRLIDYL
AEEFKKENGI DLKGDSLAVQ RLKEAAEKAK IELSSSQQTE VNLPYITADA TGPKHLVVKL
SRAKLESLVE ELVKRSLEPM KVALKDANLS ASEIDEVILV GGQTRMPMVQ AKVSEFFGKE
PRKDVNPDEA VAMGAALQGA VLSGDVKDVL LLDVTPLTLG IETMGGVATP LIEKNTTIPT
KKSQVFSTAE DNQTAVTIHV VQGERKQASA NKSLGRFDLA DIPPSPRGLP QIEVTFDIDA
NGILHVSAKD KATGKEQSIR ITASSGLDEG EIEKMVRDAE ANAEADKQFE ALVTARNTAE
GLANATRKTL EEAGDKASDD EKAAIESALT EVDEAIKGDD VEAIDAATKK LTEASGGLAE
KMYAEQAAQA QGAESDAEPK DASDDVVDAE FEEVKDDDKK
//
