HSP72_USTMA
ID HSP72_USTMA Reviewed; 645 AA.
AC P18694; A0A0D1DX88; Q4P7X2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Heat shock 70 kDa protein 2;
GN Name=UMS2; ORFNames=UMAG_03791;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90.
RX PubMed=2792075; DOI=10.1002/j.1460-2075.1989.tb03596.x;
RA Holden D.W., Kronstad J.W., Leong S.A.;
RT "Mutation in a heat-regulated hsp70 gene of Ustilago maydis.";
RL EMBO J. 8:1927-1934(1989).
CC -!- MISCELLANEOUS: UMS2 is essential for vegetative growth.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; CM003149; KIS68211.1; -; Genomic_DNA.
DR PIR; S05375; S05375.
DR RefSeq; XP_011390235.1; XM_011391933.1.
DR AlphaFoldDB; P18694; -.
DR SMR; P18694; -.
DR STRING; 5270.UM03791P0; -.
DR PRIDE; P18694; -.
DR EnsemblFungi; KIS68211; KIS68211; UMAG_03791.
DR GeneID; 23564150; -.
DR KEGG; uma:UMAG_03791; -.
DR VEuPathDB; FungiDB:UMAG_03791; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P18694; -.
DR OMA; ESYAYHM; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000000561; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
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 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; Nucleotide-binding; Reference proteome; Stress response.
FT CHAIN 1..645
FT /note="Heat shock 70 kDa protein 2"
FT /id="PRO_0000078384"
FT REGION 611..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 70333 MW; AC33939400FC7FF2 CRC64;
MTKAIGIDLG TTYSCVAVWQ NDRVEVIAND QGNRTTPSYV AFTDSERLIG DAAKNQVAMN
PHNTVFDAKR LIGRKFDDAE VQSDMKHWPF EVTSVGGKPQ IRIEYKGEKK TFTPEEISSM
VLLKMRETAE AYLGGTVKDA VVTVPAYFND SQRQATKDAG IISGLNVMRI INEPTAAAIA
YGLDKKTEGE KNVLIFDLGG GTFDVSLLTI EEGIFEVKAT AGDTHLGGED FDNRLVNHFV
QEFKRKNKKD LTTNARALRR LRTACERAKR TLSSAAQTTI EIDSLFEGID FYTSITRARF
EELCGDLFSH TIEPVEKVLR DSKIDKGSVH EIVLVGGSTR IPKVQKLLTD FFNGRELNKS
INPDEAVAYG AAVQAAILSG DTSEKTQDLL LLDVAPLSMG IETAGGVFTP LIKRNTTVPT
KKSEIFSTYA DNQPGVLIQV FEGERARTKD NNLLGKFELS GIPPAPRGVP QIEVTFDVDA
NAILNVSAAE KGTGKSEKIT IRNDKGRLSS EQIEEMLKQA EQFAEEDKQA LERTQAKNGL
ESYIYNVRNT TNEPQLKDKL EAADKEALEK IVKEGIEWLD SNTTASTDEL KDKQKEIEEQ
VNPIMTKIYS AAGGAPGGMP GGAPGAAPGG AAPGGDDGPT VEELD