DNAK_ANAMM
ID DNAK_ANAMM Reviewed; 645 AA.
AC Q5PAB8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Chaperone protein DnaK {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=HSP70 {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock 70 kDa protein {ECO:0000255|HAMAP-Rule:MF_00332};
DE AltName: Full=Heat shock protein 70 {ECO:0000255|HAMAP-Rule:MF_00332};
GN Name=dnaK {ECO:0000255|HAMAP-Rule:MF_00332}; OrderedLocusNames=AM842;
OS Anaplasma marginale (strain St. Maries).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma.
OX NCBI_TaxID=234826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St. Maries;
RX PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT is skewed to two superfamilies of outer membrane proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005).
CC -!- FUNCTION: Acts as a chaperone. {ECO:0000255|HAMAP-Rule:MF_00332}.
CC -!- INDUCTION: By stress conditions e.g. heat shock. {ECO:0000255|HAMAP-
CC Rule:MF_00332}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000255|HAMAP-Rule:MF_00332}.
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DR EMBL; CP000030; AAV86762.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5PAB8; -.
DR SMR; Q5PAB8; -.
DR PRIDE; Q5PAB8; -.
DR KEGG; ama:AM842; -.
DR HOGENOM; CLU_005965_2_1_5; -.
DR OMA; ISIKRHM; -.
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; 2.60.34.10; -; 1.
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 PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW Stress response.
FT CHAIN 1..645
FT /note="Chaperone protein DnaK"
FT /id="PRO_0000225929"
FT REGION 603..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..645
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00332"
SQ SEQUENCE 645 AA; 69935 MW; 7C5834D0B53F5B56 CRC64;
MGVIMAAERI IGIDLGTTNS CVAVMEAGTA KVIENSEGSR TTPSVVAFTE NERLVGELAK
RQANINAQNT IYASKRIIGR RYDDMRDVKC PYEVFPAKNG DAWIRARGEG YSPVQIGAFV
LEKIKETAER YFGAPVKKAV ITVPAYFNDA QRQATKDAGT IAGLDVVRII NEPTAAALAY
GLDKGDKQRT IVVYDLGGGT FDVSVLEIAE GVFEVKATNG DTKLGGEDFD NAVMEHMMES
FKQETGIDLH NDPMAVQRIK EAAEKAKIEL SSRLETDITL PFISSDSTGA KHLSLKLTRA
KFEGLVSELI ERTIEPCKKA LDDAGIKDTS KIDEVVLVGG MTRMPKVIQR VKDFFGGKEP
CKGVNPDEVV AIGAAIQGGI LTGDVRDVLL LDVAPLSLGI ETLGGVFTPL IERNTTIPTK
KSQVFSTAED GQTAVTIKVY QGERKMAVDN KLLGQFSLEG IPSAPRGIPQ IEVTFDIDAN
GIVHVSAKDK ASGKEQTIKI QSSGGLSEEE IKKMVQDAQD RAEEDEKRKK RVELKNSAEA
LIHSTEKSLN DYGDKISSAD KSGIEAAIKE LRECLSNDDS SSDVIQQKYD ALMQLSMKLG
EAAYSAQKDS GTSTDSTASD TSGNPEERVV DSEYQEIKKD DEDKK