ID   BIP_ASPNG               Reviewed;         672 AA.
AC   P83616; O13280; O14453;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2003, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000305};
DE            EC=3.6.4.10 {ECO:0000250|UniProtKB:P11021};
DE   AltName: Full=Immunoglobulin heavy chain-binding protein homolog {ECO:0000305};
DE            Short=BiP {ECO:0000305};
DE   Flags: Precursor;
GN   Name=bipA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 9089 / N402 {ECO:0000269|PubMed:9370263};
RX   PubMed=9370263; DOI=10.1016/s0378-1119(97)00290-4;
RA   van Gemeren I.A., Punt P.J., Drint-Kuyvenhoven A., Broekhuijsen M.P.,
RA   van't Hoog A., Beijersbergen A., Verrips C.T., van den Hondel C.A.M.J.J.;
RT   "The ER chaperone encoding bipA gene of black Aspergilli is induced by heat
RT   shock and unfolded proteins.";
RL   Gene 198:43-52(1997).
CC   -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC       multimeric protein complexes inside the ER. Is required for secretory
CC       polypeptide translocation. May physically associate with SEC63 protein
CC       in the endoplasmic reticulum and this interaction may be regulated by
CC       ATP hydrolysis. {ECO:0000250|UniProtKB:P16474}.
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; EC=3.6.4.10;
CC         Evidence={ECO:0000250|UniProtKB:P11021};
CC   -!- ACTIVITY REGULATION: The chaperone activity is regulated by ATP-induced
CC       allosteric coupling of the nucleotide-binding (NBD) and substrate-
CC       binding (SBD) domains. In the ADP-bound and nucleotide-free (apo)
CC       states, the two domains have little interaction. In contrast, in the
CC       ATP-bound state the two domains are tightly coupled, which results in
CC       drastically accelerated kinetics in both binding and release of
CC       polypeptide substrates. J domain-containing co-chaperones stimulate the
CC       ATPase activity and are required for efficient substrate recognition.
CC       {ECO:0000250|UniProtKB:P11021}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000250|UniProtKB:P16474, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC   -!- INDUCTION: By heat shock and tunicamycin. Not induced by carbon source
CC       starvation. {ECO:0000269|PubMed:9370263}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|RuleBase:RU003322, ECO:0000305}.
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DR   EMBL; Y08868; CAA70091.1; -; Genomic_DNA.
DR   AlphaFoldDB; P83616; -.
DR   SMR; P83616; -.
DR   STRING; 5061.CADANGAP00008595; -.
DR   PRIDE; P83616; -.
DR   VEuPathDB; FungiDB:An11g04180; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1111800; -.
DR   VEuPathDB; FungiDB:ATCC64974_90280; -.
DR   VEuPathDB; FungiDB:M747DRAFT_295101; -.
DR   eggNOG; KOG0100; Eukaryota.
DR   GO; GO:0099021; C:cortical endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; NAS:UniProtKB.
DR   GO; GO:0034099; C:luminal surveillance complex; IEA:EnsemblFungi.
DR   GO; GO:0031965; C:nuclear membrane; IEA:EnsemblFungi.
DR   GO; GO:0099020; C:perinuclear endoplasmic reticulum lumen; IEA:EnsemblFungi.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
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:0070880; P:fungal-type cell wall beta-glucan biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0036498; P:IRE1-mediated unfolded protein response; IEA:EnsemblFungi.
DR   GO; GO:0000742; P:karyogamy involved in conjugation with cellular fusion; 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; IDA:UniProtKB.
DR   GO; GO:0032940; P:secretion by cell; NAS:UniProtKB.
DR   GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IEA:EnsemblFungi.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IEA:EnsemblFungi.
DR   CDD; cd10241; HSPA5-like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR042050; BIP_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; PS00014; ER_TARGET; 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; Chaperone; Endoplasmic reticulum; Hydrolase;
KW   Nucleotide-binding; Signal; Stress response.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..672
FT                   /note="Endoplasmic reticulum chaperone BiP"
FT                   /id="PRO_0000013578"
FT   REGION          145..299
FT                   /note="Nucleotide-binding (NBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   REGION          419..519
FT                   /note="Substrate-binding (SBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   MOTIF           669..672
FT                   /note="Prevents secretion from ER"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT   BINDING         57..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         246..248
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         312..319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
FT   BINDING         383..386
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P11021"
SQ   SEQUENCE   672 AA;  73459 MW;  C701807FCE08C175 CRC64;
     MARISHQGAA KPFTAWTTIF YLLLVFIAPL AFFGTAHAQD ETSPQESYGT VIGIDLGTTY
     SCVGVMQNGK VEILVNDQGN RITPSYVAFT DEERLVGDAA KNQYAANPRR TIFDIKRLIG
     RKFDDKDVQK DAKHFPYKVV NKDGKPHVKV DVNQTPKTLT PEEVSAMVLG KMKEIAEGYL
     GKKVTHAVVT VPAYFNDAQR QATKDAGTIA GLNVLRVVNE PTAAAIAYGL DKTGDERQVI
     VYDLGGGTFD VSLLSIDNGV FEVLATAGDT HLGGEDFDQR VMDHFVKLYN KKNNVDVTKD
     LKAMGKLKRE VEKAKRTLSS QMSTRIEIEA FHNGEDFSET LTRAKFEELN MDLFKKTLKP
     VEQVLKDAKV KKSEVDDIVL VGGSTRIPKV QALLEEFFGG KKASKGINPD EAVAFGAAVQ
     GGVLSGEEGT GDVVLMDVNP LTLGIETTGG VMTKLIPRNT VIPTRKSQIF STAADNQPTV
     LIQVYEGERS LTKDNNLLGK FELTGIPPAP RGVPQIEVSF DLDANGILKV HASDKGTGKA
     ESITITNDKG RLSQEEIDRM VAEAEEFAEE DKAIKAKIEA RNTLENYAFS LKNQVNDENG
     LGGQIDEDDK QTILDAVKEV TEWLEDNAAT ATTEDFEEQK EQLSNVAYPI TSKLYGSAPA
     DEDDEPSGHD EL