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Database: UniProt
Entry: I0GX16_ACTM4
LinkDB: I0GX16_ACTM4
Original site: I0GX16_ACTM4 
ID   I0GX16_ACTM4            Unreviewed;       618 AA.
AC   I0GX16;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
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:BAL85303.1};
GN   OrderedLocusNames=AMIS_830 {ECO:0000313|EMBL:BAL85303.1};
OS   Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS   JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL85303.1, ECO:0000313|Proteomes:UP000007882};
RN   [1] {ECO:0000313|EMBL:BAL85303.1, ECO:0000313|Proteomes:UP000007882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC   NCIMB 12654 / NRRL B-3342 / UNCC 431
RC   {ECO:0000313|Proteomes:UP000007882};
RA   Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA   Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT   "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT   102363).";
RL   Submitted (FEB-2012) 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; AP012319; BAL85303.1; -; Genomic_DNA.
DR   RefSeq; WP_014440203.1; NC_017093.1.
DR   AlphaFoldDB; I0GX16; -.
DR   STRING; 512565.AMIS_830; -.
DR   KEGG; ams:AMIS_830; -.
DR   PATRIC; fig|512565.3.peg.86; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_11; -.
DR   OMA; ISIKRHM; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000007882; 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; 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:UP000007882};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          567..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          224..251
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          481..508
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         175
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   618 AA;  65953 MW;  51A3DF304A64B3AB CRC64;
     MARAVGIDLG TTNSCVSVLE GGEPTVIANA EGSRTTPSIV AFARNGEVLV GEVAKRQAVT
     NPDRTIRSVK REVGTNWSID IDGKKYTPQE ISARVLMKLK RDSEAYLGET ITDAVITVPA
     YFNDAQRQAT KEAGEIAGLN VLRIVNEPTA AALAYGLDKG SKEQTVLVFD LGGGTFDVSL
     LELGDGVIEV KSTSGDNHLG GDDWDQRIID HLVKTFRGEH GIDLSQDKMA LQRLREAAEK
     AKIELSAATT TSINLPYITA GANGPLHLDT SLSRAEFQRM TQDLLDRCKG PFESAIKDAD
     VKLSDIDHVI LVGGSTRMPA VTELVQSLIG REPNKGVNPD EVVAVGAALQ AGVLKGEVKD
     VLLLDVTPLS LGIETKGGIM HKLVERNTTI PAHRSEVYTT ADDNQPSVLI QVYQGEREMA
     AYNKKLGTFE LSGIAPAPRG VPQIEVSFDI DANGIVHVSA KDLGTGKEQK MTITGGSALP
     KEDIERMMRD AQDHADDDKK RREDAEARNL AEQLQWQTEK FLAESGDKLP EENKSKISEA
     LGELRGALGG TDIEKIKSAH ERLSQVSQEA GSLLYSQGEA PQAGPEAGGA PGGATGAGPS
     AGGNDDVVDA EIVEDDKK
//
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