ID S3A7F1_9MICO Unreviewed; 628 AA.
AC S3A7F1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ORFNames=HMPREF1529_01114 {ECO:0000313|EMBL:EPD84511.1};
OS Microbacterium sp. oral taxon 186 str. F0373.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1203549 {ECO:0000313|EMBL:EPD84511.1, ECO:0000313|Proteomes:UP000014414};
RN [1] {ECO:0000313|EMBL:EPD84511.1, ECO:0000313|Proteomes:UP000014414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0373 {ECO:0000313|EMBL:EPD84511.1,
RC ECO:0000313|Proteomes:UP000014414};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Kirega A., Dewhirst F.D.,
RA Izard J., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Microbacterium sp. oral taxon 186 F0373.";
RL Submitted (MAY-2013) 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}.
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:EPD84511.1}.
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DR EMBL; ATCC01000006; EPD84511.1; -; Genomic_DNA.
DR RefSeq; WP_016464036.1; NZ_KE150457.1.
DR AlphaFoldDB; S3A7F1; -.
DR PATRIC; fig|1203549.3.peg.1110; -.
DR HOGENOM; CLU_005965_2_4_11; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000014414; 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; 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};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 584..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 229..256
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 487..514
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 176
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 628 AA; 67284 MW; 90C976E0943E0424 CRC64;
MARAVGIDLG TTNSVVSVLE GGEPKVIANA EGFRTTPSVV AFTKDGEVLV GETAKRQAVT
NVDRTLSSVK RHMGTDWKTQ AIDGKQYTPQ EISARILQKL KRDAEEYLGD SVTDAVITVP
AYFNDAERQA TKDAGEIAGL NVLRIINEPT AAALAYGLDK GKEDELILVF DLGGGTFDVS
LLEVGKDDDF STIQVRATAG DNRLGGDDWD QRVVDYLIKQ FKDTTGVDVS GDKIALQRLK
EAAEQAKKEL SSSSSTSINL PYLSLTDSGP VSLSETLTRA KFEDLTKDLL DRTKKPFNDV
IAEAGIKVGD IDHVVLVGGS TRMPQVTELV KQLTGGKEPN KGVNPDEVVA VGAALQAGVL
KGERKDVLLI DVTPLSLGIE TKGGIMTKLI ERNTAIPTKR SETFTTADDN QPSVAIQVFQ
GERDFTRDNK PLGTFELTGI APAPRGIPQI EVTFDIDANG IVHVSAKDKG TGKEQSMTIT
GGSSLPKDDI ERMVREAEEH AAEDKKRREA AEVRNQAETL SYSIEKLIKD NEDKLPAEVK
TSVQADVDAL KTALAGDDED AVKNAFDKLN ASQQQLGEAI YASAQAAGEP ADPTVADPGN
GSVPNPEEDV IDAEVVEDED DKKPGTGK
//
