ID K6WAQ0_9MICO Unreviewed; 642 AA.
AC K6WAQ0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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:GAB78922.1};
GN ORFNames=AUCHE_17_01360 {ECO:0000313|EMBL:GAB78922.1};
OS Austwickia chelonae NBRC 105200.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Austwickia.
OX NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB78922.1, ECO:0000313|Proteomes:UP000008495};
RN [1] {ECO:0000313|EMBL:GAB78922.1, ECO:0000313|Proteomes:UP000008495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB78922.1,
RC ECO:0000313|Proteomes:UP000008495};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL Submitted (AUG-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}.
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:GAB78922.1}.
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DR EMBL; BAGZ01000017; GAB78922.1; -; Genomic_DNA.
DR RefSeq; WP_006503679.1; NZ_BAGZ01000017.1.
DR AlphaFoldDB; K6WAQ0; -.
DR STRING; 100225.SAMN05421595_0137; -.
DR eggNOG; COG0443; Bacteria.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000008495; 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; 2.
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:UP000008495};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT COILED 230..257
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 488..515
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 642 AA; 68050 MW; FF4403193B81BFA2 CRC64;
MARAVGIDLG TTNSAVSVLE GNEPTIIANA EGGRTTPSVV AFSKNGEVLV GEIAKRQAVT
NVDRTIRSVK RHMGTDWNQE IDGKKYTAQE ISARTLMKLK RDAESYLGEP VTDAVITVPA
YFDDAERQAT KEAGEIAGLN VLRIVNEPTA AALAYGLDKG KEDELILVFD LGGGTFDVSL
LEVGKDPEDG FSTIQVRATH GDNKLGGDDW DERIVQHLLT TVKNQTGVDL ANDKIAMQRL
RDAAEQAKKE LSSSTSTNIS LQYLSMSENG PIHLDENLSR VQFEQMTSDL LDRCKTPFEQ
VIKDAGVSVG EIDHVVLVGG STRMPAVTEV VKKLTGGKEP NKGVNPDEVV AVGASLQAGV
LKGERKDVLL IDVTPLSLGI ETKGGLMTKL IERNTAIPTK RSEVFTTAED NQPSVLIQVF
QGERELASAN KALGTFELTG IAPAPRGIPQ IEVTFDIDPN GIVHVSAKDR GTGKEQSMTI
SGGSALPKEE IERMVKEAEQ HAEEDKKRRE QAEARNTAEQ LVYSTDKFLA DSGDKVPADT
KKPVEEALAD LKAALAKTGD EAVSSEELNA KVTKLNEVSQ KMGSAIYAAA QAEGEQKPAG
PGAAGAAGAA GAAGAAAGFA AGSAGKDDVI DAEVVDEGDT KK
//
