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Database: UniProt
Entry: A0A086Y3W5_9RHOB
LinkDB: A0A086Y3W5_9RHOB
Original site: A0A086Y3W5_9RHOB 
ID   A0A086Y3W5_9RHOB        Unreviewed;       638 AA.
AC   A0A086Y3W5;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
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   ECO:0000313|EMBL:KFI28965.1};
GN   ORFNames=CG50_12280 {ECO:0000313|EMBL:KFI28965.1};
OS   Paenirhodobacter enshiensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paenirhodobacter.
OX   NCBI_TaxID=1105367 {ECO:0000313|EMBL:KFI28965.1, ECO:0000313|Proteomes:UP000028824};
RN   [1] {ECO:0000313|EMBL:KFI28965.1, ECO:0000313|Proteomes:UP000028824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW2-9 {ECO:0000313|EMBL:KFI28965.1,
RC   ECO:0000313|Proteomes:UP000028824};
RA   Wang D., Wang G.;
RT   "Genome of Paenirhodobacter enshiensis DW2-9.";
RL   Submitted (MAR-2014) 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:KFI28965.1}.
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DR   EMBL; JFZB01000005; KFI28965.1; -; Genomic_DNA.
DR   RefSeq; WP_036635499.1; NZ_JFZB01000005.1.
DR   AlphaFoldDB; A0A086Y3W5; -.
DR   STRING; 1105367.CG50_12280; -.
DR   eggNOG; COG0443; Bacteria.
DR   OrthoDB; 9766019at2; -.
DR   Proteomes; UP000028824; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000028824};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_00332}.
FT   REGION          517..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..638
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          246..273
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        517..533
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..638
FT                   /note="Basic and acidic residues"
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   638 AA;  68731 MW;  4DF1AE92A820C412 CRC64;
     MSKVIGIDLG TTNSCVAIMD GSQPRVIENS EGARTTPSIV AFTDNERLVG QAAKRQAVTN
     PTNTVFAVKR LIGRKVGDAE VQKDKKLVPY AIVDGGNGDA WVEVRGDKFS PAQISAIILQ
     KMKETAESYL GEPVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
     DKKETKTIAV YDLGGGTFDI TILEIDDGLF EVKSTNGDTF LGGEDFDMRI VHYLADEFKK
     EHGVDLTADK MALQRLKEAA EKAKIELSSS QQTDINQPFI SMDMKTGTPL HMVMKLTRAK
     LENLVGDLIK KSLKPCEAAL KDAGVSKGEI DEVVLVGGMT RMPKVVEAVT EFFGKEPHKG
     VNPDEVVAMG AAIQAGVLQG DVKDVVLLDV TPLSLGIETL GGVFTRLIDR NTTIPTKKSQ
     VFSTAEDNQN AVTIRVFQGE REMAADNKML GQFNLEQIPP APRGVPQIEV TFDIDANGIV
     SVSAKDKGTG KSQQITIQAS GGLSDEDIEK MVKDAEANAE ADKKRKELVE TKNQGESLLD
     STRKSLKEHG DKVDPSTVEA IEFACTALEE ALKTEDAGKI KGAISNLTDA SMKLGEAIYK
     AQQSEGEGHA DDDDAPRAAD DDNIVDADFE DMGDNKRK
//
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