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Database: UniProt
Entry: E1X0G7_HALMS
LinkDB: E1X0G7_HALMS
Original site: E1X0G7_HALMS 
ID   E1X0G7_HALMS            Unreviewed;       642 AA.
AC   E1X0G7;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
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:CBW27993.1};
GN   OrderedLocusNames=BMS_3243 {ECO:0000313|EMBL:CBW27993.1};
OS   Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS   (Bacteriovorax marinus).
OC   Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC   Halobacteriovoraceae; Halobacteriovorax.
OX   NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW27993.1, ECO:0000313|Proteomes:UP000008963};
RN   [1] {ECO:0000313|Proteomes:UP000008963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC   {ECO:0000313|Proteomes:UP000008963};
RX   PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA   Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA   Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA   Williams H.N., Stine O.C.;
RT   "A small predatory core genome in the divergent marine Bacteriovorax
RT   marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL   ISME J. 7:148-160(2013).
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; FQ312005; CBW27993.1; -; Genomic_DNA.
DR   RefSeq; WP_014245763.1; NC_016620.1.
DR   AlphaFoldDB; E1X0G7; -.
DR   STRING; 862908.BMS_3243; -.
DR   KEGG; bmx:BMS_3243; -.
DR   PATRIC; fig|862908.3.peg.3099; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_7; -.
DR   Proteomes; UP000008963; 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:SF541; CHAPERONE PROTEIN DNAK; 1.
DR   PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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}; Reference proteome {ECO:0000313|Proteomes:UP000008963};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          587..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          248..275
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        589..603
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         198
FT                   /note="Phosphothreonine; by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ   SEQUENCE   642 AA;  68634 MW;  7F39371A74750C6F CRC64;
     MGKIIGIDLG TTNSCVSVLE NGKYKIIANA EGHNTTPSVI GFANNGDTLV GQVAKRQAVT
     NPTKTLYGIK RLIGRKADTP EAKKFADVAP FEIFANKNGD AWVKVDGKEM SPQEISAIVL
     QKLKKAAEDY LGEEVSEAVI TVPAYFNDAQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
     LDSKVDKNIA VFDLGGGTFD ISILEITTDG VFEVKATNGD TFLGGENFDE DIINYLAEEF
     NKTEGIDLRK DQMALQRLKE AAEKAKHELS NVNSTDVNLP FITADASGPK HLNINLSRAK
     FESLIAKDLE ALAKPCLTCL EDSGLDRNEI HEVILVGGST RMPAVQERVK EIFGKEASKG
     VNPDEVVAAG AAIQGGVLAG DVKDVLLLDV TPLSLGIETL GGVMTKLIDK NTTIPVKKSQ
     VFSTAQDNQP AVSIHVLQGE REFANDNKTL GRFDLTGIAP APRGVPQVEV IFDIDANGIV
     NVSAVDKATG NKQEVKITAG SGLTDDEIER MVKEAEANKD ADSKRREIVD TRNSLDALIL
     SCEKMIKDGG DKIAEGDKKE LEAAIEAAKG KLQSEVLDEL KAEQERLQNA SHKIAQQMYQ
     QPGAEGQPGP DMGAGQAGAG ADAGQAKKKD DDDVVDADFK EV
//
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