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Database: UniProt
Entry: M7NYY8_9GAMM
LinkDB: M7NYY8_9GAMM
Original site: M7NYY8_9GAMM 
ID   M7NYY8_9GAMM            Unreviewed;       638 AA.
AC   M7NYY8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:EMR12426.1};
GN   ORFNames=MPL1_10307 {ECO:0000313|EMBL:EMR12426.1};
OS   Methylophaga lonarensis MPL.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR12426.1, ECO:0000313|Proteomes:UP000012019};
RN   [1] {ECO:0000313|EMBL:EMR12426.1, ECO:0000313|Proteomes:UP000012019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MPL {ECO:0000313|EMBL:EMR12426.1,
RC   ECO:0000313|Proteomes:UP000012019};
RX   PubMed=23661481;
RA   Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P.,
RA   Murrell J.C., Shouche Y.S.;
RT   "Draft Genome Sequence of Methylophaga lonarensis MPLT, a Haloalkaliphilic
RT   (Non-Methane-Utilizing) Methylotroph.";
RL   Genome Announc. 1:E00202-13(2013).
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}.
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:EMR12426.1}.
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DR   EMBL; APHR01000056; EMR12426.1; -; Genomic_DNA.
DR   RefSeq; WP_009727031.1; NZ_APHR01000056.1.
DR   AlphaFoldDB; M7NYY8; -.
DR   STRING; 1286106.MPL1_10307; -.
DR   PATRIC; fig|1286106.3.peg.2060; -.
DR   eggNOG; COG0443; Bacteria.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000012019; 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   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:UP000012019};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          605..638
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   638 AA;  68559 MW;  A37AB279B21BA7F2 CRC64;
     MGKIIGIDLG TTNSCVAVLE DGKARVIENS EGDRTTPSIV AFTKDNEVLV GQSAKRQAVT
     NPSNTLYGIK RLIGRKFKED VVQRDIDMVP YKIVEADNGD AWVQANDKKM APPEISARVL
     MKMKKTAEEF LGEPVTEAVV TVPAYFNDSQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
     MDKKRGDSTV VVYDLGGGTF DVSIIEIADI EGEHQFEVLA TNGDTFLGGE DFDQRIIDFL
     VSEFKKDQGV DLSKDPLALQ RLKDAAEKAK IELSSSQQTD INLPYITADA SGPKHMEIRL
     TRAKLESLVD DLITRSLEPC KVALKDAGLS VSEISEVILV GGQTRMPKVQ EAVKELFGKE
     PRRDVNPDEA VAVGAAIQAA VLAGDVKDVL LLDVTPLSLG IETMGGVMTK LVEKNTTIPT
     KAQQVFSTAD DNQPAVTIHV LQGEREMASA NKSLGRFDLA DIPPAPRGVP QIEVTFDIDA
     NGILNVSAKD KATGKEQSIV IKASSGLSDE EVEKMVKDAE AHAEEDRKFH ELVTARNTAD
     GLIHATNKSL KDLGDKVDAA EKSAIESAIE SLQEALKGED KADIEAKTNT LSEAAAKLAE
     RAYAENAEAG DGAASESAAE ASDDVVDAEF EEVNDDKK
//
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