ID V6HYH1_9LEPT Unreviewed; 643 AA.
AC V6HYH1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, 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 ECO:0000313|EMBL:EQA62970.1};
GN ORFNames=LEP1GSC062_4203 {ECO:0000313|EMBL:EQA62970.1};
OS Leptospira alexanderi serovar Manhao 3 str. L 60.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049759 {ECO:0000313|EMBL:EQA62970.1, ECO:0000313|Proteomes:UP000018747};
RN [1] {ECO:0000313|EMBL:EQA62970.1, ECO:0000313|Proteomes:UP000018747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L 60 {ECO:0000313|EMBL:EQA62970.1,
RC ECO:0000313|Proteomes:UP000018747};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Hartskeerl R.A., Ahmed A.,
RA van der Linden H., Goris M.G.A., Vinetz J.M., Sutton G.G., Nierman W.C.,
RA Fouts D.E.;
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:EQA62970.1}.
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DR EMBL; AHMT02000026; EQA62970.1; -; Genomic_DNA.
DR RefSeq; WP_010577002.1; NZ_AHMT02000026.1.
DR AlphaFoldDB; V6HYH1; -.
DR STRING; 100053.GCA_002009845_02219; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000018747; 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.
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 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 602..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 643 AA; 68930 MW; 5FDF6BE302C17327 CRC64;
MSKEKIIGID LGTTNSVVSV MEGGDPVVIQ NSEGARTTPS IVAFTAKGEN LVGQFAKNQA
ITNAVNTIRS AKRFIGRRIS ECESEMKHVS YKVIRSGNEG VKFETSAGEF TPQEISARVL
MKMKQTAEDY LGQKVTKAVI TVPAYFNDEQ RQATKDAGRI AGLEVERIIN EPTAAALAYG
FDKKNVNSKI AVYDLGGGTF DISILELADG VFEVKSTNGD THLGGDDFDM AIMEWMISEF
KNQTGIDISA DKNTVQRLKE AAEKAKIELS GTMSTQINLP FITADASGPK HLDMTLSRAK
FDQLTKSLVD RTRIPCENAL RDAGLKASDI NEVILVGGSI RIPAVQELVK QIFGKEPNKS
VNPDEVVAVG AAIQGGVLAG EVSDVLLLDV TPLSLGIETL GGVMTKLIER NTTIPTKKSQ
VFSTAADNQS AVSIHVLQGE REMASANRTL GRFDLIGIPP APRGVPQIEV TFDIDANGIV
HVSAKDLGTG KEQKIRIESS SGLSEDEIQK MVKDAEAHAA ADKAQREVIE AKNELDTLAY
SLEKTVNEAG DKIGASEKQL ATDEIKRARE AIESNDKARM ESAKASISKI ASDIATKIYS
QGAPGAEQAA GSTGPDQGQN DQGKNNGEKV VDADYTVVDD EKK
//
