ID A0A0F4LSG7_9LACO Unreviewed; 616 AA.
AC A0A0F4LSG7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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:KJY61500.1};
GN ORFNames=JF72_07900 {ECO:0000313|EMBL:KJY61500.1};
OS Lactobacillus apis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=303541 {ECO:0000313|EMBL:KJY61500.1, ECO:0000313|Proteomes:UP000033682};
RN [1] {ECO:0000313|EMBL:KJY61500.1, ECO:0000313|Proteomes:UP000033682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hma11 {ECO:0000313|EMBL:KJY61500.1,
RC ECO:0000313|Proteomes:UP000033682};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (JAN-2015) 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:KJY61500.1}.
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DR EMBL; JXLG01000005; KJY61500.1; -; Genomic_DNA.
DR RefSeq; WP_046307030.1; NZ_KQ034000.1.
DR AlphaFoldDB; A0A0F4LSG7; -.
DR STRING; 303541.JF72_07900; -.
DR PATRIC; fig|303541.3.peg.947; -.
DR HOGENOM; CLU_005965_2_4_9; -.
DR Proteomes; UP000033682; 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}; Reference proteome {ECO:0000313|Proteomes:UP000033682};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 474..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 482..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..602
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 616 AA; 66375 MW; 39DDE25E23A35D01 CRC64;
MSKVIGIDLG TTNSAVAVLE GKEPKIITNP EGNRTTPSVV AFKDGEIQVG EVAKRQAITN
PNTISSIKRH MGEADYKVKI GDKAYTPQEI SAMILQYIKK FSEDYLGEKV TEAVITVPAY
FNDAQRQATK DAGKIAGLDV KRIINEPTAS SLAYGLDKDA EDEKVLVYDL GGGTFDVSVL
QLGDGVFQVL STNGDTNLGG DDFDNKIIDW LVQNFKDENG VDLSKDKMAL QRLKDAAEKA
KKDLSGVSST HISLPFISAG ESGPLHLETD LTRAKFDELT ADLVDRTKIP FDNALKDADL
TVNDIDKVIL NGGSTRIPAV QEAVKRWAGK APDHSINPDE AVALGAAIQG GVISGDVKDV
VLLDVTPLSL GIETMGGVFT KLIEKNTTIP TSKSQIFSTA ADNQPAVDVH VLQGERPMAA
DDKTLGRFEL TDIPAAPRGV PQIQVTFDID KNGIVNVSAK DMGTGKEQKI TIKSSSGLSD
EEIQKMQKEA EEHAEEDKKK KEEVDLRNEV DQLIFSTEKT LDDVKDKVSE EDTKKVKDAL
EALKKAQKDN NLDEMKTKKD ELSKVAQDLA VKLYQANGGA QGAEGQAGPQ NPGSQDGNST
GGSADEGEFH KVDPDK
//
