ID G2IYR8_PSEUL Unreviewed; 638 AA.
AC G2IYR8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:BAK75671.1};
GN OrderedLocusNames=NH8B_0839 {ECO:0000313|EMBL:BAK75671.1};
OS Pseudogulbenkiania sp. (strain NH8B).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Pseudogulbenkiania.
OX NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK75671.1, ECO:0000313|Proteomes:UP000001274};
RN [1] {ECO:0000313|Proteomes:UP000001274}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX PubMed=22038961; DOI=10.1128/JB.06127-11;
RA Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT Pseudogulbenkiania sp. strain NH8B.";
RL J. Bacteriol. 193:6395-6396(2011).
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; AP012224; BAK75671.1; -; Genomic_DNA.
DR RefSeq; WP_014086132.1; NC_016002.1.
DR AlphaFoldDB; G2IYR8; -.
DR STRING; 748280.NH8B_0839; -.
DR KEGG; pse:NH8B_0839; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000001274; 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}; 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:UP000001274};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 604..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..638
FT /note="Basic and acidic residues"
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; 69081 MW; C6AF53B4AF23E3EB CRC64;
MGKIIGIDLG TTNSCVSVIE NGHPKVIENA EGTRTTPSII AYMEDGEILV GAPAKRQAVT
NPKNTLYAIK RLIGRRFEEK EVQKDIDLMP FEITKAKNGD SWVKVRDQEL APPQISAEVL
RKMKKTAEDY LGEEVTEAVI TVPAYFNDSQ RQATKDAGRI AGLDVKRIIN EPTAAALAFG
LAKQEGDRKI AVYDLGGGTF DISIIEIADV EGEHQFEVLS TNGDTFLGGE DFDQRLIDYI
VTEFKREQGV DLKNDVMALQ RLKDAAEKAK IELSSASQTE VNLPYITMDA TGPKHLAMKI
TRAKFESLVE DLIARSIEPC RVALKDAGVS INDIADVILV GGQTRMPKVQ EAVKEFFGKE
PRKDVNPDEA VAVGAAIQGS VLSGDRKDVL LLDVTPLSLG IETLGGIMTK LIQKNTTIPT
KAQQTFSTAD DNQTAVTIHV LQGEREKASA NKSLGQFNLS DIPAAPRGMP QIEVTFDIDA
NGILHVSAKD KGTGKEAKIT IQASSGLSEE EIQRMVKDAE VNAEEDKKLH ELVQARNQGE
GMIHSVKKSL AEHGDKISAE EKAAIEAALK EAEEVVKGDD KDAIDAKVQA LMTASHKLAE
QMYSQAQGEA GAGQPAGAGN KDEGDVVDAE FEEVKDKK
//
