BIP_KLULA
ID BIP_KLULA Reviewed; 679 AA.
AC P22010; Q6CRF1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=GRP78; Synonyms=BIP; OrderedLocusNames=KLLA0D09559g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2243798; DOI=10.1093/nar/18.21.6438;
RA Lewis M.J., Pelham H.R.B.;
RT "The sequence of the Kluyveromyces lactis BiP gene.";
RL Nucleic Acids Res. 18:6438-6438(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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: 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 -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH00584.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X54709; CAA38516.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00584.1; ALT_FRAME; Genomic_DNA.
DR PIR; S13122; S13122.
DR RefSeq; XP_453488.1; XM_453488.1.
DR AlphaFoldDB; P22010; -.
DR SMR; P22010; -.
DR STRING; 28985.XP_453488.1; -.
DR PRIDE; P22010; -.
DR EnsemblFungi; CAH00584; CAH00584; KLLA0_D09559g.
DR GeneID; 2892944; -.
DR KEGG; kla:KLLA0_D09559g; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_0_1; -.
DR InParanoid; P22010; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0034099; C:luminal surveillance complex; 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: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; IEA:EnsemblFungi.
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; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Endoplasmic reticulum; Hydrolase;
KW Nucleotide-binding; Reference proteome; Signal; Stress response.
FT SIGNAL 1..43
FT /evidence="ECO:0000250"
FT CHAIN 44..679
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_0000013582"
FT REGION 147..301
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 421..521
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 652..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 676..679
FT /note="Prevents secretion from ER"
FT COMPBIAS 664..679
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 248..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 314..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 385..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
SQ SEQUENCE 679 AA; 74448 MW; 530BC47F3224E0F2 CRC64;
MFSARKSSVG WLVSSLAVFY VLLAVIMPIA LTGSQSSRVV ARAAEDHEDY GTVIGIDLGT
TYSCVAVMKN GKTEILANEQ GNRITPSYVS FTDDERLIGD AAKNQAASNP KNTIFDIKRL
IGLQYNDPTV QRDIKHLPYT VVNKGNKPYV EVTVKGEKKE FTPEEVSGMI LGKMKQIAED
YLGKKVTHAV VTVPAYFNDA QRQATKDAGA IAGLNILRIV NEPTAAAIAY GLDKTEDEHQ
IIVYDLGGGT FDVSLLSIEN GVFEVQATAG DTHLGGEDFD YKLVRHFAQL FQKKHDLDVT
KNDKAMAKLK REAEKAKRSL SSQTSTRIEI DSFFNGIDFS ETLTRAKFEE LNLALFKKTL
KPVEKVLKDS GLQKEDIDDI VLVGGSTRIP KVQQLLEKFF NGKKASKGIN PDEAVAYGAA
VQAGVLSGEE GVEDIVLLDV NALTLGIETT GGVMTPLIKR NTAIPTKKSQ IFSTAVDNQK
AVRIQVYEGE RAMVKDNNLL GNFELSDIRA APRGVPQIEV TFALDANGIL TVSATDKDTG
KSESITIAND KGRLSQDDID RMVEEAEKYA AEDAKFKAKS EARNTFENFV HYVKNSVNGE
LAEIMDEDDK ETVLDNVNES LEWLEDNSDV AEAEDFEEKM ASFKESVEPI LAKASASQGS
TSGEGFEDED DDDYFDDEL
