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Database: UniProt
Entry: G5GHE9_9FIRM
LinkDB: G5GHE9_9FIRM
Original site: G5GHE9_9FIRM 
ID   G5GHE9_9FIRM            Unreviewed;       620 AA.
AC   G5GHE9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
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=HMPREF9333_00989 {ECO:0000313|EMBL:EHI55946.1};
OS   Johnsonella ignava ATCC 51276.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Johnsonella.
OX   NCBI_TaxID=679200 {ECO:0000313|EMBL:EHI55946.1, ECO:0000313|Proteomes:UP000003011};
RN   [1] {ECO:0000313|EMBL:EHI55946.1, ECO:0000313|Proteomes:UP000003011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51276 {ECO:0000313|EMBL:EHI55946.1,
RC   ECO:0000313|Proteomes:UP000003011};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA   Baranova O.V., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA   Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Johnsonella ignava ATCC 51276.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHI55946.1}.
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DR   EMBL; ACZL01000015; EHI55946.1; -; Genomic_DNA.
DR   RefSeq; WP_005540336.1; NZ_JH378831.1.
DR   AlphaFoldDB; G5GHE9; -.
DR   STRING; 679200.HMPREF9333_00989; -.
DR   PATRIC; fig|679200.3.peg.1041; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_9; -.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000003011; 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.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00332};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, 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:UP000003011};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          590..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          223..250
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         174
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   620 AA;  66013 MW;  96DFB0E683C3A146 CRC64;
     MSKIIGIDLG TTNSCVAVME GGKPVVIPNS EGSRTTPSVV AFTKAGERLV GEPAKRQAVT
     NSDRTISSIK RHMGTDYKAT IDGKAYTPQE ISAMILQKLK ADAEAYLGEK VTEAVITVPA
     YFNDAQRQAT KDAGKIAGLD VKRIINEPTA AALAYGLDNE KEQKIMVYDL GGGTFDVSII
     EIGDGVIEVL ATNGDTRLGG DDFDNKITNW MVGEFKKTEG VDLSGDKMAM QRLKEAAEKA
     KKELSTSTTT NINLPFITAT SEGPKHLDMT LTRAKFDELT SDLIERTALP VQNALNDAGI
     KASDLGKVLL VGGSTRMINA QEKVKQLTSH EPSKTLNPDE CVAIGACIQG GKLAGDAGAG
     DILLLDVTPL SLSIETMGGV ATKLIERNTT IPTKKSQIFS TAADNQSAVD IHVVQGERQF
     ARDNKTLGQF RLDGILPARR GVPQIEVTFD IDANGIVNVS AKDLGTGKEQ HITITSGSNM
     SDSDIEKAVK EAAEFEAQDK KRKEAIDTRN DADSMVFQTE KALEEVGDKI DANDKAAVEA
     ELSALKEAIN RAPAESMTDD QIADIKANKE KLMETAQKLF AKVYENAQAG AQAAGSADST
     AGQGGAEPDG DVVDGDFKEV
//
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