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Database: UniProt
Entry: E1QXU7_OLSUV
LinkDB: E1QXU7_OLSUV
Original site: E1QXU7_OLSUV 
ID   E1QXU7_OLSUV            Unreviewed;       630 AA.
AC   E1QXU7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 71.
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   OrderedLocusNames=Olsu_0077 {ECO:0000313|EMBL:ADK67211.1};
OS   Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS   NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK67211.1, ECO:0000313|Proteomes:UP000000333};
RN   [1] {ECO:0000313|EMBL:ADK67211.1, ECO:0000313|Proteomes:UP000000333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC   VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX   PubMed=21304694; DOI=10.4056/sigs.1082860;
RA   Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA   Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL   Stand. Genomic Sci. 3:76-84(2010).
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; CP002106; ADK67211.1; -; Genomic_DNA.
DR   RefSeq; WP_013250963.1; NZ_JQCO01000002.1.
DR   AlphaFoldDB; E1QXU7; -.
DR   STRING; 633147.Olsu_0077; -.
DR   GeneID; 78511560; -.
DR   KEGG; ols:Olsu_0077; -.
DR   PATRIC; fig|633147.7.peg.1572; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_11; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000000333; 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; 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   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:UP000000333};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          602..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         197
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   630 AA;  67679 MW;  1C6CBEDC42575B26 CRC64;
     MGKILGIDLG TTNSAMAVLE GGEPTIIVNA EGERTTPSVI GFRADGDRIV GKAAKNQAVT
     NPKNTVFSIK RFMGRRYNEV SSELKTVPYT VKAGTGDRAV VEIEGEDFTP EQISAMTLAK
     MKADAEKYLG ESVTDAVITV PAYFNDAQRQ ATKDAGKIAG LNVQRIVNEP TAAALAYGLD
     KKDIDQKVLV FDLGGGTFDV SLLDLADGVV EVLATNGDNH LGGDDWDQKV IDWMADKFQS
     ENGIDLRRDP MTLQRLKEAA ENAKKELSSA QQTEINLPFI AMDANGPKNL MYTLTRAEFE
     RITRDLLDRC KGPVTKALRD AGLQISDVNE VILVGGSSRM PAVQDLVKTM TGKQPNMSVN
     PDEVVADGAA IQGGVLTGDV LGILLLDVTP LSLGVETMGG VMTKMIDRNT TIPTSKTEIY
     STAADNQTSV EINVLQGERE MAADNKSLGK FNLTGIPSAR RGVPQIEVTF DIDANGIVKV
     TAKDKGTGKQ QQITISGSTA LSDDEVDRMV KDAESHAEED KKHKDEIEVR NQTDSLCYST
     EQTLKDLGDK VPADMKKQVE DAVTDAKKAL DGTDIDAIKS AGEKLQEVGH KLAEIVYSDT
     AAQASGDQAT GGADDVVDAD YEVVDDKDER
//
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