ID   LHS1_CANGA              Reviewed;         889 AA.
AC   Q6FU50;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=Heat shock protein 70 homolog LHS1;
DE            EC=3.6.1.-;
DE   Flags: Precursor;
GN   Name=LHS1; OrderedLocusNames=CAGL0F06369g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Chaperone required for protein translocation and folding in
CC       the endoplasmic reticulum. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; CR380952; CAG59168.1; -; Genomic_DNA.
DR   RefSeq; XP_446244.1; XM_446244.1.
DR   AlphaFoldDB; Q6FU50; -.
DR   SMR; Q6FU50; -.
DR   STRING; 284593.Q6FU50; -.
DR   GlyCosmos; Q6FU50; 7 sites, No reported glycans.
DR   EnsemblFungi; CAGL0F06369g-T; CAGL0F06369g-T-p1; CAGL0F06369g.
DR   GeneID; 2887859; -.
DR   KEGG; cgr:CAGL0F06369g; -.
DR   CGD; CAL0130854; CAGL0F06369g.
DR   VEuPathDB; FungiDB:CAGL0F06369g; -.
DR   eggNOG; KOG0104; Eukaryota.
DR   HOGENOM; CLU_005965_5_0_1; -.
DR   InParanoid; Q6FU50; -.
DR   OMA; DYGQQNI; -.
DR   Proteomes; UP000002428; Chromosome F.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IEA:EnsemblFungi.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:EnsemblFungi.
DR   CDD; cd10230; HYOU1-like_NBD; 1.
DR   Gene3D; 3.30.30.30; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR45639; HSC70CB, ISOFORM G-RELATED; 1.
DR   PANTHER; PTHR45639:SF3; HYPOXIA UP-REGULATED PROTEIN 1; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW   Nucleotide-binding; Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..889
FT                   /note="Heat shock protein 70 homolog LHS1"
FT                   /id="PRO_0000013555"
FT   REGION          811..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           886..889
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        843..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..889
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        462
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        502
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        716
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        752
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   889 AA;  99634 MW;  58CD2D752B2DD11F CRC64;
     MKLSILFLFA IAVQAAFLGI DYGQQSIKAM VVSPKAMMEI VLTPEAKRKD TSGICIRNVN
     GVLERHYGNS IGSLVTRFPQ NTAMHLRSLL GKSMNDKDTI ESYLRENPGA NLTSTTRNTI
     AITIDGVEYP VEQLVAMNLQ EIIDRANQHI KETDTTGIDF VEQVGIAIPE QFNQAQRQAL
     LDALALTSVK DEAVLVSDGL SVAIDYALKR PDLEINVPQY YIVFDVGTSA AKATLFSLTQ
     PEDLSSPIKI EIGAFDSEAT VGGSKFIAAI ADIVEDKFLE KNTKITRKSL VENPRARAKI
     IQAAEKAKLV LSANNEAIIS IESLVDDIDF RTTIARSEFQ DIFEDNKHTV VKAIKGAIGN
     QLWDDNISLE DISGVILSGG SSRVPMVQEE IAKLVGEEKI LKNVNADETV INGATLKGLK
     YFGSFKTKPL DITERSLFDY SVEMSGESSS KTVFEKGTKF PNESSILYKA PKKFGKELKF
     DLFESDTRIL SNIVDTTVSS KNWTSACKKG QLYLNVTFDL DSNRVFKIKD ITVLCDSDGN
     AKEEEFEFID VINDVTKATD VMPLSNAEIR QLSNAITSWN RKDRERKRVQ ESLNVLEAEL
     YDCRSFIEEF EEKLGEEEFE TLKSFTAFVK EKLEYLEDNS ADMSKKDIEK LVRETRSQRD
     TLSRFYNSLD AALGSKDFQK LVDTASKSIK KYKEIESKNL ADLENKAEKF NVIGLNVTEK
     YNSILSKMSF SSIRRSSEEN IKTLAGLIDE VNESIKSKAI DDESLENLIK TKLAFEELIN
     TLDLENRQWT YQHQLVMKEL KKMYNKKMKA IKKQEKQNEN EENGDDEGDD EDETKTKKYL
     KEATSSGDSS TIKEEDSTGS NEAGNKGDEE DEEEEEDDSS AGNVFDDEL
//