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Database: UniProt
Entry: E1NRX6_9LACO
LinkDB: E1NRX6_9LACO
Original site: E1NRX6_9LACO 
ID   E1NRX6_9LACO            Unreviewed;       615 AA.
AC   E1NRX6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 55.
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:EFO71134.1};
GN   ORFNames=HMPREF9211_0903 {ECO:0000313|EMBL:EFO71134.1};
OS   Lactobacillus iners LactinV 01V1-a.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=879297 {ECO:0000313|EMBL:EFO71134.1, ECO:0000313|Proteomes:UP000003648};
RN   [1] {ECO:0000313|EMBL:EFO71134.1, ECO:0000313|Proteomes:UP000003648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LactinV 01V1-a {ECO:0000313|EMBL:EFO71134.1,
RC   ECO:0000313|Proteomes:UP000003648};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC       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:EFO71134.1}.
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DR   EMBL; AEHQ01000029; EFO71134.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1NRX6; -.
DR   Proteomes; UP000003648; 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   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};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, 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          575..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          223..250
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        575..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   615 AA;  66334 MW;  DFB7AF24C5A552EB CRC64;
     MSKVIGIDLG TTNSAVAVLE GKEPKIITNP EGNRTTPSVV AFKNGEIQVG EVAKRQAITN
     PNTISSIKRH MGEEGYKVKV DGKEYTPQEI SAMILQYIKK FAEDYLGEPV KDAVITVPAY
     FNDAQRQATK DAGKIAGLNV QRIINEPTAS SLAYGLDKDE KDEKILVYDL GGGTFDVSVL
     ELGDGVFQVL STNGDTNLGG DDFDNAIIDW LIENFKKENG VDLSSDKMAL QRLKDAAEKA
     KKDLSGISST HISLPFISAG ESGPLHLEAD LSRAKFDELT HDLVARTKIP FDNALKDAGL
     SVSDIDKVIL NGGSTRIPAV QEAVKQWAGK DPDHSINPDE AVALGAAVQG GVITGDVKDI
     VLLDVTPLSL GIETMGGVFT KLIDKNTTIP TSKSQIFSTA ADNQPAVDVH VLQGERPMAA
     DNKTLGRFQL TDIPAAPRGV PQIQVTFDID KNGIVNVSAK DMGTGKEQKI TIKSSTGLSD
     EEIKRMQKEA EEHAEEDKKK KEEADLRNEV DQVIFSTNKT LEEVKGKLSD NDIKPVEDAL
     EALKKAQKDN DLVAMKEKKD ALSKVAQDLA VKLYQKQNTQ GQSGTKENGN GNDKGTDGNG
     NSTVDGDFHK VDPDK
//
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