ID A0A0P1F9W4_THAGE Unreviewed; 642 AA.
AC A0A0P1F9W4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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_2 {ECO:0000313|EMBL:CUH64896.1};
GN Synonyms=dnaK {ECO:0000256|HAMAP-Rule:MF_00332};
GN ORFNames=TG4357_01563 {ECO:0000313|EMBL:CUH64896.1};
OS Thalassovita gelatinovora (Thalassobius gelatinovorus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Thalassovita.
OX NCBI_TaxID=53501 {ECO:0000313|EMBL:CUH64896.1, ECO:0000313|Proteomes:UP000051587};
RN [1] {ECO:0000313|EMBL:CUH64896.1, ECO:0000313|Proteomes:UP000051587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 4357 {ECO:0000313|EMBL:CUH64896.1,
RC ECO:0000313|Proteomes:UP000051587};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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}.
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DR EMBL; CYSA01000015; CUH64896.1; -; Genomic_DNA.
DR RefSeq; WP_058262283.1; NZ_FOFW01000002.1.
DR AlphaFoldDB; A0A0P1F9W4; -.
DR STRING; 53501.SAMN04488043_102112; -.
DR OrthoDB; 9766019at2; -.
DR Proteomes; UP000051587; 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:UP000051587};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00332}.
FT REGION 600..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 246..273
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 610..634
FT /note="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 642 AA; 69190 MW; 1A43B77D7E01F1E7 CRC64;
MSKVIGIDLG TTNSCVSIMD GSQPKVIENS EGARTTPSIV AFTDDERLVG QAAKRQAVTN
ASNTIFGVKR LIGRRFDDEH LAKDKKNLPF AVVDGGNGDA WVEAKSEKYS PSQISAFILG
KMKETAESYL GEEVTQAVIT VPAYFNDAQR QATKDAGKIA GLEVLRIINE PTAAALAYGL
DKKETHTIAV YDLGGGTFDV TILEIDDGLF EVKSTNGDTF LGGEDFDMRI VSYLASEFKK
EHGVDLTKDK MALQRLKEAA EKAKIELSSS QQTEINQPFI SMDPNGGQPL HMVMKLTRAK
LESLVSDLIK ASIKPCQAAL KDAGLTTSDI DEVVLVGGMT RMPRVVEEVT KFFGKEPHKG
VNPDEVVAMG AAIQAGVLQG DVKDVVLLDV TPLSLGIETL GGVFTRLIDR NTTIPTKKSQ
VFSTAEDHQS AVTIRVFQGE REMAADNKML GQFNLEDIPP APRGLPQIEV TFDIDANGIV
SVSAKDKGTG KEQNITIQAS GGLSDDEIDQ MVKDAETNAE ADKDRKEMVE ARNQAESLIH
STEKSMEEHA DKVDPTTVEA IELAIAALKD DLEKDDITAD KIKSGIQNVT ESAMKLGEAI
YKASQDEGED APADVDSDAS GGAADDDIVD ADFEDLDDDK RA
//
