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
//