ID   HSP01_PINST             Reviewed;         104 AA.
AC   P84717;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Putative heat shock protein PS1;
DE   Flags: Fragments;
OS   Pinus strobus (Eastern white pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Strobus.
OX   NCBI_TaxID=3348;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Leaf {ECO:0000269|PubMed:16529377};
RX   PubMed=16529377; DOI=10.1094/mpmi-19-0150;
RA   Smith J.A., Blanchette R.A., Burnes T.A., Jacobs J.J., Higgins L.,
RA   Witthuhn B.A., David A.J., Gillman J.H.;
RT   "Proteomic comparison of needles from blister rust-resistant and
RT   susceptible Pinus strobus seedlings reveals upregulation of putative
RT   disease resistance proteins.";
RL   Mol. Plant Microbe Interact. 19:150-160(2006).
CC   -!- FUNCTION: Putative molecular chaperone that may promote the maturation,
CC       structural maintenance and proper regulation of specific target
CC       proteins. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein is: 5.6,
CC       its MW is: 97.6 kDa. {ECO:0000269|PubMed:16529377}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000255}.
CC   -!- CAUTION: The order of the peptides shown is unknown.
CC       {ECO:0000269|PubMed:16529377}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW   Nucleotide-binding; Stress response.
FT   CHAIN           <1..>104
FT                   /note="Putative heat shock protein PS1"
FT                   /id="PRO_0000240628"
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        11
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        18
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_CONS        13..14
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        25..26
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        44..45
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        58..59
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        67..68
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        77..78
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        85..86
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_CONS        93..94
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:16529377"
FT   NON_TER         104
FT                   /evidence="ECO:0000303|PubMed:16529377"
SQ   SEQUENCE   104 AA;  11360 MW;  8F3F2AAE53E46113 CRC64;
     GVVDSNDLPL NVSELVSNAS DALDKLSSSP CVLVSGKFWD NFGKTZTVEV EDDSAEAKTL
     SKFLNAALTD KTEEVVRNWK LMNAAELLSE INRLSSSEWQ AALR