ID A0A076NLP3_9CORY Unreviewed; 614 AA.
AC A0A076NLP3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
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:AIJ34288.1};
GN ORFNames=CIMIT_10675 {ECO:0000313|EMBL:AIJ34288.1}, SAMEA4535761_02192
GN {ECO:0000313|EMBL:SNV84253.1};
OS Corynebacterium imitans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=156978 {ECO:0000313|EMBL:AIJ34288.1, ECO:0000313|Proteomes:UP000028780};
RN [1] {ECO:0000313|EMBL:AIJ34288.1, ECO:0000313|Proteomes:UP000028780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44264 {ECO:0000313|EMBL:AIJ34288.1,
RC ECO:0000313|Proteomes:UP000028780};
RA Mollmann S., Albersmeier A., Ruckert C., Tauch A.;
RT "Complete genome sequence of Corynebacterium imitans DSM 44264, isolated
RT from a five-month-old boy with suspected pharyngeal diphtheria.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SNV84253.1, ECO:0000313|Proteomes:UP000215374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13015 {ECO:0000313|EMBL:SNV84253.1,
RC ECO:0000313|Proteomes:UP000215374};
RG Pathogen Informatics;
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP009211; AIJ34288.1; -; Genomic_DNA.
DR EMBL; LT906467; SNV84253.1; -; Genomic_DNA.
DR RefSeq; WP_038592688.1; NZ_LT906467.1.
DR AlphaFoldDB; A0A076NLP3; -.
DR STRING; 156978.CIMIT_10675; -.
DR KEGG; cii:CIMIT_10675; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_4_11; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000028780; Chromosome.
DR Proteomes; UP000215374; Chromosome 1.
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; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 3.
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}; Reference proteome {ECO:0000313|Proteomes:UP000028780};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 493..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 224..251
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 493..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 175
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 614 AA; 66380 MW; F0E6B276398D4EBC CRC64;
MARAVGIDLG TTNSVVSVLE GGEPVVIANA EGSRTTPSVV AFAKNGEVLV GQSAKNQAVT
NVDRTIRSVK RHMGEDWTVN IDDKDYTPQE ISARTLQKLK RDAEAYLGDE VTDAVITVPA
YFEDAQRQAT KEAGQIAGLN VLRIVNEPTA AALAYGLEKN DSEQTILVFD LGGGTFDVSL
LEIGDGVVEV LATAGDNELG GDDWDNRIVE WLVDKFKSAQ GVDLSKDKMA MQRLREAAEK
AKIELSSSQQ ASINLPYITV DSEKNPLFLD ETLSRTEFQK ITSDLLDRTK TPFNQVIKDA
GLSLGDINHV VLVGGSTRMP AVTDLVKEMT GKEPNKSVNP DEVVALGAAL QAGVLRGDVK
DVLLLDVTPL SLGIETKGGV MTKLIERNTT IPTKRSETFT TAEDNQPSVQ IQVFQGEREM
ASANKLLGSF ELAGIAPAPR GVPQIEVTFD IDANGIVSVS AKDKATGKEN TIKIQDGSGL
SQEEIDRMIK DAEQHADEDK KRREEQETRN GAESAAYQTR KFMEDNEDKL PEDLKTRVTE
AADAVDEALK GDDLEAVKSA VEKLNTESQE LGKVLYEAQA NEGATQADAP TDDDVVDAEV
VEEDAEESKD SDNK
//