DNAK_NITHX
ID DNAK_NITHX Reviewed; 632 AA.
AC Q1QRU1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=Nham_0155;
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Nitrobacter.
OX NCBI_TaxID=323097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP000319; ABE61056.1; -; Genomic_DNA.
DR RefSeq; WP_011508762.1; NC_007964.1.
DR AlphaFoldDB; Q1QRU1; -.
DR SMR; Q1QRU1; -.
DR STRING; 323097.Nham_0155; -.
DR PRIDE; Q1QRU1; -.
DR EnsemblBacteria; ABE61056; ABE61056; Nham_0155.
DR KEGG; nha:Nham_0155; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; DKMVLQR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000001953; 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 Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
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 PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..632
FT /note="Chaperone protein DnaK"
FT /id="PRO_1000059617"
FT REGION 524..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 632 AA; 68161 MW; 2551A7E947B63DEF CRC64;
MGKVIGIDLG TTNSCVAVMD GKTPKVIENA EGMRTTPSIV AFSDDGERLV GQPAKRQAVT
NPERTIFAVK RLIGRRYDDP TVEKDKHLVP YKIAKAGNGD AWVEVDGKTY SPSQISAFTL
QKMKETAEAH LGQKVDQAVI TVPAYFNDAQ RQATKDAGKI AGLEVLRIIN EPTAAALAYG
LDKAKQGTIA VYDLGGGTFD VSILEIGDGV FEVKSTNGDT FLGGEDFDMR LVSYLADEFQ
KEQGINLRND KLALQRLKEA AEKAKIELSS TTQTEINLPF ITADQSGPKH LTMKLTRAKF
EALVDDLVQK TIEPCRKALK DAGLTAGEIG EVVLVGGMTR MPKVQEVVKQ LFGKEPHKGV
NPDEVVAIGA AIQAGVLQGD VKDVLLLDVT PLSLGIETLG GVFTRIIDRN TTIPTKKSQV
FSTAEDSQNA VTIRVFQGER EMAADNKILG QFDLMGIPPA PRGMPQIEVT FDIDANGIVN
VSAKDKATGK EQQIRIQASG GLSEADIDKM VKDAEANAIE DKKRREAVDA KNHADSLVHS
TEKALAEHGS KIEDSERRAI EDAVSDLKEA LKGDDAEAIK AKTNTLAQAS MKLGEAMYKQ
QAEADAAKDA AKDDVVDAEF TEVDDDKNKK SA