ID A0A0A1GTZ6_9LACO Unreviewed; 624 AA.
AC A0A0A1GTZ6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 ORFNames=LOOC260_111880 {ECO:0000313|EMBL:BAP85727.1};
OS Paucilactobacillus hokkaidonensis JCM 18461.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1291742 {ECO:0000313|EMBL:BAP85727.1, ECO:0000313|Proteomes:UP000031620};
RN [1] {ECO:0000313|EMBL:BAP85727.1, ECO:0000313|Proteomes:UP000031620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LOOC260 {ECO:0000313|EMBL:BAP85727.1,
RC ECO:0000313|Proteomes:UP000031620};
RA Tanizawa Y., Tohno M., Kaminuma E., Nakamura Y., Arita M.;
RT "Complete genome sequence and analysis of Lactobacillus hokkaidonensis
RT LOOC260T.";
RL Submitted (NOV-2014) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP014680; BAP85727.1; -; Genomic_DNA.
DR RefSeq; WP_041093614.1; NZ_AP014680.1.
DR AlphaFoldDB; A0A0A1GTZ6; -.
DR STRING; 1291742.LOOC260_111880; -.
DR KEGG; lho:LOOC260_111880; -.
DR HOGENOM; CLU_005965_2_4_9; -.
DR Proteomes; UP000031620; Chromosome.
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; 2.
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 534..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 225..252
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 587..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 624 AA; 67662 MW; 30D8E94B6988B1A0 CRC64;
MASNKIIGID LGTTNSAVAV MEGKDPKIIT NPEGSRTTPS VVSFKDGETQ VGEVAKRQAI
TNPNTIVSIK SHMGDANYTV EVEGKKYTPQ EISAMILQYL KKYAEDYLGD EVTQAVITVP
AYFNDAQRQA TKDAGKIAGL DVKRIINEPT ASSLAYGLDK KDKDEKVLVY DLGGGTFDVS
ILELGDGVFQ VLSTNGDTHL GGDDFDKKII DWLVSEFKKE NGVDLAQDKM AMQRLKDAAE
KAKKDLSGVN EAQISLPFIS AGASGPLHME KSLTRAQFNQ LTVDLVEKTK QPVLNALKDA
DLSFSDVDEV ILNGGSTRIP AVQEMVKDLT GKEPNHSINP DEAVAIGAAV QGGVLTGDVK
DVVLLDVTPL SLGIETMGGV FTKLIDRNTT IPTSKSQTFS TAADNQPAVD IHVLQGERPM
AADNKTLGNF QLTDIPAAPR GVPQIQVTFD IDKNGIVNVS AKDMGTNKEQ KITIKSNSGL
SDDEIDRMMK EAKENEEADN QKKEEVDLNN EVDQLLFQVD KTLKDLKGKV SDEEVKKAED
ARDALKKAKE DKNVEDMKTK KDELNKIVQD LSVKLYQQAQ EAKDGAKGDQ ATGDDKGKSG
DDGKTVDGDF EEVNPDDKKP DDKK
//
