ID D6V1M2_9BRAD Unreviewed; 725 AA.
AC D6V1M2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 24-JAN-2024, entry version 54.
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=AfiDRAFT_1589 {ECO:0000313|EMBL:EFI53602.1};
OS Afipia sp. 1NLS2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=666684 {ECO:0000313|EMBL:EFI53602.1, ECO:0000313|Proteomes:UP000004041};
RN [1] {ECO:0000313|EMBL:EFI53602.1, ECO:0000313|Proteomes:UP000004041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLS2 {ECO:0000313|EMBL:EFI53602.1,
RC ECO:0000313|Proteomes:UP000004041};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Prakah O.,
RA Elkins J.G., Brown S.D., Palumbo A.V., Hemme C., Zhou J., Watson D.B.,
RA Jardine P.M., Kostka J.E., Green S.J., Woyke T.J.;
RT "The draft genome of Afipia sp. 1NLS2.";
RL Submitted (MAY-2010) 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:EFI53602.1}.
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DR EMBL; ADVZ01000001; EFI53602.1; -; Genomic_DNA.
DR AlphaFoldDB; D6V1M2; -.
DR eggNOG; COG0443; Bacteria.
DR Proteomes; UP000004041; 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; cd11733; HSPA9-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}; Chaperone {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 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 335..362
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 694..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 725 AA; 78062 MW; 3EC0B1985308E8D5 CRC64;
MDGGFDSSFQ DAPTGPARRS RNGLSGMLTG ENKCRRITAF TPFGPCGPYR PSYMRRSVAE
RRAWILRGLG AVRRQGPANP PQKKDRGTMG KVIGIDLGTT NSCVAVMDGK SPKVIENAEG
MRTTPSIVAF TNDGERLVGQ PAKRQAVTNP ENTIFAVKRL IGRRYDDPTV EKDKKLVPYK
IMKASNGDAW VEASGQTYSP SQVSAFILQK MKETAEAHLG QKVDQAVITV PAYFNDAQRQ
ATKDAGKIAG LEVLRIINEP TAAALAYGLD KSKQGTIAVY DLGGGTFDVS ILEIGDGVFE
VKSTNGDTFL GGEDFDMRLV GYLADEFQKE QGINLRNDKL ALQRLKEAAE KAKIELSSTT
QTEVNLPFIT ADATGPKHLT MKLTRAKFEA LVDDLVQKTI EPCRKALKDA GLSAGEVGEV
VLVGGMTRMP KIQEIVKQFF GKEPHKGVNP DEVVAIGAAI QAGVLQGDVK DVLLLDVTPL
SLGIETLGGV FTRIIERNTT IPTKKSQVFS TAEDNQGAVT IRVFQGEREM AADNKALGQF
DLMGIPPAPR GMPQIEVTFD IDANGIVNVS AKDKATGKEQ QIRIQASGGL SESEIEKMVK
DAEANAAEDK KRREAVDAKN HADALVHSTE KALAEHGGKV SEGDRKAIED ALADLKEALK
GDDSEAIKAK SNTLAQASMK LGEAMYQQQA EADAKADAAK DAAHDDVVDA EFTEVDDDKT
NKKSA
//