ID A0A024QBH0_9BACI Unreviewed; 613 AA.
AC A0A024QBH0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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:CDQ39607.1};
GN ORFNames=BN990_01912 {ECO:0000313|EMBL:CDQ39607.1};
OS Virgibacillus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ39607.1, ECO:0000313|Proteomes:UP000028875};
RN [1] {ECO:0000313|EMBL:CDQ39607.1, ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ39607.1,
RC ECO:0000313|Proteomes:UP000028875};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL Submitted (MAY-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 -!- 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:CDQ39607.1}.
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DR EMBL; CCDP010000001; CDQ39607.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024QBH0; -.
DR STRING; 1462526.BN990_01912; -.
DR eggNOG; COG0443; Bacteria.
DR Proteomes; UP000028875; 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:UP000028875};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 575..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..250
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 575..592
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 613 AA; 66739 MW; 0635D3477DA6250D CRC64;
MMSKIIGIDL GTTNSCVAVM EGGESVVIPN PEGNRTTPSV VAFKNGERQV GEVAKRQAIT
NPDTIQSIKR HMGTDYKVKI EDKEFTPQEV SAIILQHIKS YAEDYIGEPV SKAVITVPAY
FNDAERQATK DAGKIAGLEV ERIINEPTAA ALAYGIDKED EDQTILVYDL GGGTFDVSIL
DIGDGTFEVV STAGDNRLGG DDFDDVIIDH MVQEFKKENG IDLSKDKMAA QRLKDAAEKA
KKDLSGVAQT QISLPFITAG EAGPLHLEMN LTRAKFEELS SDLVERTMVP TRNALSDADL
SASDIDKVIL VGGSTRIPAV QEAIKKMIGK DPSKGVNPDE VVALGAAIQG GVLQGDVKDV
VLLDVTPLSL GIETMGSVTT KLIERNTTIP TSESQVFSTA ADNQTAVDIH VLQGEREMAA
DNKTLGRFQL TDIPPAPRGV PQIEVSFDID ANGIVNVRAK DLGTNKEQSI TIKSSSGLSD
DEVDRMVKEA EENAEADKQR REEVELRNEA DQLIFTTDKT IKDLGDNVSD EEKQKAEAAK
EELQKAIEAD DLDQIKEKKE ALQEQVQQLS VKMYEQMQQE QQAQQSQDGS GNDDDVVDAD
YQEVDDEEDK DKK
//
