ID   HSP71_PICAN             Reviewed;         645 AA.
AC   P53421;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Heat shock protein 70 1;
DE   AltName: Full=HSP72;
GN   Name=HSA1;
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RX   PubMed=8840502;
RX   DOI=10.1002/(sici)1097-0061(199607)12:9<849::aid-yea985>3.0.co;2-z;
RA   Titorenko V.I., Evers M.E., Diesel A., Samyn B., van Beeumen J.,
RA   Roggenkamp R.O., Kiel J.A.K.W., van der Klei I.J., Veenhuis M.;
RT   "Identification and characterization of cytosolic Hansenula polymorpha
RT   proteins belonging to the Hsp70 protein family.";
RL   Yeast 12:849-857(1996).
CC   -!- FUNCTION: Acts as a chaperone. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By heat shock.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; Z29379; CAA82570.1; -; Genomic_DNA.
DR   PIR; S41372; S41372.
DR   AlphaFoldDB; P53421; -.
DR   SMR; P53421; -.
DR   PRIDE; P53421; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Nucleotide-binding; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..645
FT                   /note="Heat shock protein 70 1"
FT                   /id="PRO_0000078376"
FT   REGION          612..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   645 AA;  70138 MW;  00901307086680E9 CRC64;
     MSKAVGIDLG TTYSCVAHFV NDRVEIIAND QGNRTTPSFV AFTDTERLIG DAAKNQAAMN
     PANTVFDAKR LIGRKFDDPE VQNDIKHFPF KVVEKGGKPH IQVEFKGETK VFTPEEISSM
     VLTKMKETAE SYMGGKVTDA VITVPAYFND SQRQATKDAG LIAGLNVLRI INEPTAAAIA
     YGLDKKEQGK GEQNILIFDL GGGTFDVSLL SIDEGIFEVK ATAGDTHLGG EDFDNRLVNH
     FANEFKRKYK KDLTTNQRAL RRLRTACERA KRTLSSSAQT SVEIDSLYEG IDFYTSITRA
     RFEELCQDLF RSTLDPVEKV MRDGKLDKSQ VAEIVLVGGS TRIPKIQKLV SDFFNGKEPN
     KSINPDEAVA YGAAVQAAIL TGDTSSKTQD LLLLDVAPLS LGIETAGGVM TKLIPRNTTI
     PTKKSEIFST YSDNQPGVLI QVYEGERAKT KDNNLLGKFE LSGIPPAPRG VPQIEVTFDI
     DANGILNVSA VEKGTGKSQK ITITNDKGRL SKEEIDRMVA EAEKYKEEDE KEAARIAAKN
     GLESYAYSLK QTASEKQFEE KVDASKRESL NKAIEETISW LDNNQSATTD EYEDKRKELE
     GIANDALKDL YAAGGVPGGA APGGFPGAGG AAPGADQGPS VEEVD