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Database: UniProt
Entry: A0A117LSF2_9FIRM
LinkDB: A0A117LSF2_9FIRM
Original site: A0A117LSF2_9FIRM 
ID   A0A117LSF2_9FIRM        Unreviewed;       611 AA.
AC   A0A117LSF2;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Chaperone protein DnaK {ECO:0000256|ARBA:ARBA00014415, 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   ORFNames=XD84_1013 {ECO:0000313|EMBL:KUK64917.1};
OS   Desulfotomaculum sp. 46_80.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=1641375 {ECO:0000313|EMBL:KUK64917.1, ECO:0000313|Proteomes:UP000053828};
RN   [1] {ECO:0000313|Proteomes:UP000053828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000256|ARBA:ARBA00002290,
CC       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:KUK64917.1}.
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DR   EMBL; LGGF01000015; KUK64917.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A117LSF2; -.
DR   PATRIC; fig|1641375.3.peg.530; -.
DR   Proteomes; UP000053828; 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; 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};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          577..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          223..250
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        594..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   611 AA;  66219 MW;  24887C8A9759E6C8 CRC64;
     MAKVIGIDLG TTNSCVAVME GGEAVVIPNA EGGRTTPSVV GFSKTGERLV GQVAKRQAVS
     NHERTISSIK RQMGYDYKVT IDEKDYTPQE ISAMILQKMK TDAGAYLGDK VEKAVITVPA
     YFTDAQRQAT KDAGRIAGLE VLRIINEPTA AALAYGLDRG EDHTVLVFDL GGGTFDVSIL
     DLGEGVFEVR ATNGNNRLGG DDFDQRIMDW LVAEFKKENG IDLSKDKMAL QRLKEAAEKA
     KVELSTLTST SISLPFITAD ASGPRHLEIN LTRARFEEMT ADLIEKTMGP TRQALSDAGL
     KPSDIHRILL VGGATRMPAV QENIRRFLGK EPHKGINPDE CVAIGAAIQA GVLAGEVKDV
     LLLDVTPLSL GIETLGGVFT RLIERNTTIP TSKSQNFSTA ADGQTTVEIH ILQGERQMAM
     DNKTLGRFQL TGIPPAPRGI PQIEVKFDID VNGIVHVSAK DIGTGKAQSI TVTGGTSLNK
     DEIEKMVKDS EQYAEVDRKR KEEAELHNQA DSLIYQAEKT IKDLGDKADK SLVGQVEKSA
     ADLKDALASG DLEIIKKRIE ELTKPLYDLS AAMYQQQSAQ QAEGAQGNQP GDEKVVDADY
     EVKDEENNLK E
//
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