ID N1UT83_9MICC Unreviewed; 623 AA.
AC N1UT83;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Chaperone protein DnaK {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:EMY33631.1};
GN ORFNames=D477_013832 {ECO:0000313|EMBL:EMY33631.1};
OS Arthrobacter crystallopoietes BAB-32.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1246476 {ECO:0000313|EMBL:EMY33631.1, ECO:0000313|Proteomes:UP000010729};
RN [1] {ECO:0000313|EMBL:EMY33631.1, ECO:0000313|Proteomes:UP000010729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-32 {ECO:0000313|EMBL:EMY33631.1,
RC ECO:0000313|Proteomes:UP000010729};
RX PubMed=23833141;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Desai S.M., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of Arthrobacter crystallopoietes Strain BAB-32,
RT Revealing Genes for Bioremediation.";
RL Genome Announc. 1:e00452-13(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:EMY33631.1}.
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DR EMBL; ANPE02000162; EMY33631.1; -; Genomic_DNA.
DR RefSeq; WP_005270036.1; NZ_ANPE02000162.1.
DR AlphaFoldDB; N1UT83; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000010729; 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; HEAT SHOCK PROTEIN 70KDA; 1.
DR PANTHER; PTHR19375:SF184; STRESS-70 PROTEIN, MITOCHONDRIAL; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000010729};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 582..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 228..255
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 623 AA; 66579 MW; 444CD6C7288CA5AB CRC64;
MSRAVGIDLG TTNSVVSVLE GGEPTVIANA EGGRTTPSVV AFSKSGEVLV GEIAKRQAVN
NIERTIASVK RHMGTDWKKE VDGKNYTAQE ISARILQKLK HDAEAYLGEK VTDAVITVPA
YFNDAERQAT KEAGEIAGMN VLRIVNEPTA AALAYGLDKG KEDELILVFD LGGGTFDVSL
LEVGKDEDDF STIQVRATAG DNRLGGDDWD QRVVDYLLKQ AKSKGADLSN DKIALQRLKE
AAEQAKKELS SASSTNISLQ YLSVTPEGPV HLDEHLSRAK FQELTADLLE RTKKPFHDVI
KEAGIKVSDI DHIVLVGGST RMPAVYDLVK EMAGGKEPNK GVNPDEVVAV GAALQAGVLK
GERKDVLLID VTPLSLGIET KGGVMTKLIE RNTAIPTKRS ETFTTADDNQ PSVAIQVFQG
EREFTRDNKP LGTFELTGIA PAPRGVPQVE VTFDIDANGI VHVSAKDKGT GAEQSMTITG
GTALSKDDID RMVREAEEHA AEDKKRREAA DIRNSAEQLA YSVDKLLADN DEKLPAEVKT
EVKADVDALK AALEKQDNDD EVKAAFEKLQ ASQTKLGEAI YSQAQAGAPG EGAPAGDGAA
GAGSANADED IVDAEVVDEE EKK
//
