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Database: UniProt
Entry: HSP7S_PEA
LinkDB: HSP7S_PEA
Original site: HSP7S_PEA 
ID   HSP7S_PEA               Reviewed;         706 AA.
AC   Q02028;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Stromal 70 kDa heat shock-related protein, chloroplastic;
DE   Flags: Precursor;
GN   Name=HSP70; Synonyms=ST70;
OS   Pisum sativum (Garden pea) (Lathyrus oleraceus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf;
RX   PubMed=16653016; DOI=10.1104/pp.100.2.1048;
RA   Marshall J.S., Keegstra K.;
RT   "Isolation and characterization of a cDNA clone encoding the major Hsp70 of
RT   the pea chloroplastic stroma.";
RL   Plant Physiol. 100:1048-1054(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Dark skinned Perfection; TISSUE=Leaf;
RA   Casey R., Creissen G., Domoney C., Forster C., Matta N.;
RL   Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Interacts with newly imported chloroplast proteins to assist
CC       in their maturation.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; L03299; AAA33637.1; -; mRNA.
DR   EMBL; X69213; CAA49147.1; -; Genomic_DNA.
DR   PIR; S32818; S32818.
DR   AlphaFoldDB; Q02028; -.
DR   SMR; Q02028; -.
DR   DIP; DIP-735N; -.
DR   IntAct; Q02028; 3.
DR   TCDB; 3.A.9.1.1; the chloroplast envelope protein translocase (cept or tic-toc) family.
DR   GO; GO:0009570; C:chloroplast stroma; 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   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   CDD; cd10234; HSPA9-Ssq1-like_NBD; 1.
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; Chloroplast; Nucleotide-binding; Plastid; Stress response;
KW   Transit peptide.
FT   TRANSIT         1..67
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           68..706
FT                   /note="Stromal 70 kDa heat shock-related protein,
FT                   chloroplastic"
FT                   /id="PRO_0000013550"
FT   REGION          663..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        692..706
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   706 AA;  75515 MW;  B3E0A1F4C9735D7B CRC64;
     MASSAQIHGL GTASFSSLKK PSSISGNSKT LFFGQRLNSN HSPFTRAAFP KLSSKTFKKG
     FTLRVVSEKV VGIDLGTTNS AVAAMEGGKP TIITNAEGQR TTPSVVAYTK NGDRLVGQIA
     KRQAVVNPEN TFFSVKRFIG RKMSEVDEES KQVSYRVIRD DNGNVKLDCP AIGKSFAAEE
     ISAQVLRKLV DDASKFLNDK VTKAVVTVPA YFNDSQRTAT KDAGRIAGLE VLRIINEPTA
     ASLAYGFERK NNETILVFDL GGGTFDVSVL EVGDGVFEVL STSGDTHLGG DDFDKRVVDW
     LAGDFKRDEG IDLLKDKQAL QRLTETAEKA KMELSSLSQT NISLPFITAT ADGPKHIETT
     LTRAKFEELC SDLLDRLRTP VENSLRDAKL SIKDIDEVIL VGGSTRIPAV QELVKKLIGK
     DPNVTVNPDE VVALGAAVQA GVLAGDVSDI VLLDVSPLSL GLETLGGVMT KIIPRNTTLP
     TSKSEVFSTA ADGQTSVEIN VLQGEREFVR DNKSLGSFRL DGIPPAPRGV PQIEVKFDID
     ANGILSVAAI DKGTGKKQDI TITGASTLPG DEVERMVSEA ERFSKEDKEK REAIDTKNQA
     DSVVYQTEKQ LKELGEKVPA PVKEKVEAKL GELKEAITGG STQTIKDALA ALNQEVMQLG
     QSLYNQPGAA GQAGPTPPGS ESGPSESSGK EGPEGDVIDA DFTDSK
//
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