ID L7CFE1_RHOBT Unreviewed; 645 AA.
AC L7CFE1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
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 ORFNames=RBSWK_03491 {ECO:0000313|EMBL:ELP32550.1};
OS Rhodopirellula baltica SWK14.
OC Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC Rhodopirellula.
OX NCBI_TaxID=993516 {ECO:0000313|EMBL:ELP32550.1, ECO:0000313|Proteomes:UP000010959};
RN [1] {ECO:0000313|EMBL:ELP32550.1, ECO:0000313|Proteomes:UP000010959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWK14 {ECO:0000313|EMBL:ELP32550.1,
RC ECO:0000313|Proteomes:UP000010959};
RX PubMed=23273849;
RA Wegner C.E., Richter-Heitmann T., Klindworth A., Klockow C., Richter M.,
RA Achstetter T., Glockner F.O., Harder J.;
RT "Expression of sulfatases in Rhodopirellula baltica and the diversity of
RT sulfatases in the genus Rhodopirellula.";
RL Mar. Genomics 0:0-0(2012).
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:ELP32550.1}.
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DR EMBL; AMWG01000099; ELP32550.1; -; Genomic_DNA.
DR RefSeq; WP_007326035.1; NZ_AMWG01000099.1.
DR AlphaFoldDB; L7CFE1; -.
DR SMR; L7CFE1; -.
DR PATRIC; fig|993516.3.peg.3722; -.
DR Proteomes; UP000010959; 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 509..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..283
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 199
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00332"
SQ SEQUENCE 645 AA; 69423 MW; FBCDF71F3C3A645B CRC64;
MAQGEKIIGI DLGTTNSVVA IMEGSEPKVI PNPEGNRLTP SVVAFTDKQE TIVGEPARRQ
AVTNPKRTVY SAKRFMGRRH NEVQSEEKMV PYGITGGPGD YVKIQVGDSE YTPQEISAKV
LRKLKESAES YLGHKVNKAV ITVPAYFNDA QRQATKDAGQ IAGLEVARII NEPTAAALAY
GLDKKKDESI IVFDLGGGTF DVSVLEVADS GDEEQESRVF QVVSTSGDTH LGGDDFDEAL
INYVASEFQK DNGIDLRNDA MALQRLQEAC EKAKKELSTL PETDINLPFI TMDASGPKHL
TMKITRSKFE ELIDALVERC RGPVLQALKD AGMDPKDIDE VVLVGGSTRV PKVREVVKSI
FGKDPHQGVN PDEVVAVGAA IQGSVLAGDR NDVLLLDVTP LTLGIETEGG VMTALVERNT
TIPAEKKNVF STAADNQTAV TVRVFQGERK MANANRLLAE FNLEDIPAAP RGVPQIEVKF
DIDQNGILSV SAKELKTGKE ANVEIKDSGA LSDSDIEQMQ KDAEANAEED KRQFELVEAR
NKVNQQVYQL EKLMGENDDK LSDDDKAPMN AAIEKVKKAA EGDDLAEIKA ASDELEAASQ
AFSKVLYEKT DAAGEAGADA AGAAGATAGG GDDDDAIDAE FEVKE
//
