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Database: UniProt
Entry: K2EN71_9BACT
LinkDB: K2EN71_9BACT
Original site: K2EN71_9BACT 
ID   K2EN71_9BACT            Unreviewed;       641 AA.
AC   K2EN71;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   13-SEP-2023, entry version 41.
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=ACD_8C00041G0003 {ECO:0000313|EMBL:EKE20201.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKE20201.1};
RN   [1] {ECO:0000313|EMBL:EKE20201.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
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:EKE20201.1}.
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DR   EMBL; AMFJ01002862; EKE20201.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2EN71; -.
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   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
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};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          600..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          503..530
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   641 AA;  69324 MW;  28F37C25764E6988 CRC64;
     MSKILGIDLG TTNSAMAIVT GGKPEILENK EGNRTTPSMV AISKTGERLV GLLAKRQSVT
     NPANTLYSIK RLIGRAYHDA EVQRDEKLMP YKIVHAGENV KVTMGDKDYS PQEISAMILG
     KLKADAEEKL GEKITDAVIT VPAYFDDAQR KATKEAGEIA GFNVRRVINE PTAAALAYGF
     DKKADEKIAV YDLGGGTFDI SILEVGGDTV EVKSTNGDTH LGGDDFDQII IQWIIDEFKK
     QEGIDLSKDP LSLQRIKEAA EKAKIELSTA QETEINQPFI TSDASGPKHL VMKMSRAKLE
     ELVGDLVQKT LEPVKKALAD SKLSTSDINE VVMVGGMTRM PLVLQTVEKF FGKKPNISVN
     PDEVVALGAA IQGGVLEGSV KDVLLLDVTP LTLGIETMGG ISTPLIERNT TVPTSKTQTF
     STAADNQPGV EIHVLQGERE VASGNKTLGK FLLDGIPPAP RGVPQIEVEF DIDANGILNV
     TAKDKATGKS QSIKIEASSG LSKEEIEKMK KDAELHAEED KNKKELVEAR NMADTLVYTT
     EKALKEAGDK VTDEEKKPVT DAIEELNKVK NGEDLNDIKA KTETLSQAAQ KIGEKLYAAA
     QEKEKADKEA NAGAEGADVK EAEVDADKKE EGEEKKDEDK K
//
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