ID F0XBZ3_GROCL Unreviewed; 663 AA.
AC F0XBZ3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000256|ARBA:ARBA00019933};
DE EC=3.6.4.10 {ECO:0000256|ARBA:ARBA00012554};
DE AltName: Full=Immunoglobulin heavy chain-binding protein homolog {ECO:0000256|ARBA:ARBA00031728};
GN ORFNames=CMQ_679 {ECO:0000313|EMBL:EFX03751.1};
OS Grosmannia clavigera (strain kw1407 / UAMH 11150) (Blue stain fungus)
OS (Graphiocladiella clavigera).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Leptographium.
OX NCBI_TaxID=655863 {ECO:0000313|Proteomes:UP000007796};
RN [1] {ECO:0000313|EMBL:EFX03751.1, ECO:0000313|Proteomes:UP000007796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=kw1407 / UAMH 11150 {ECO:0000313|Proteomes:UP000007796};
RX PubMed=21262841; DOI=10.1073/pnas.1011289108;
RA DiGuistini S., Wang Y., Liao N.Y., Taylor G., Tanguay P., Feau N.,
RA Henrissat B., Chan S.K., Hesse-Orce U., Alamouti S.M., Tsui C.K.M.,
RA Docking R.T., Levasseur A., Haridas S., Robertson G., Birol I., Holt R.A.,
RA Marra M.A., Hamelin R.C., Hirst M., Jones S.J.M., Bohlmann J., Breuil C.;
RT "Genome and transcriptome analyses of the mountain pine beetle-fungal
RT symbiont Grosmannia clavigera, a lodgepole pine pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2504-2509(2011).
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:0000256|ARBA:ARBA00002226}.
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:0000256|ARBA:ARBA00001629};
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000256|RuleBase:RU003322}.
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DR EMBL; GL629765; EFX03751.1; -; Genomic_DNA.
DR RefSeq; XP_014173233.1; XM_014317758.1.
DR AlphaFoldDB; F0XBZ3; -.
DR STRING; 655863.F0XBZ3; -.
DR GeneID; 25980261; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_0_1; -.
DR InParanoid; F0XBZ3; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000007796; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 3.30.30.30; -; 1.
DR Gene3D; 3.30.420.40; -; 2.
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:SF144; ENDOPLASMIC RETICULUM CHAPERONE BIP; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003322};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003322};
KW Reference proteome {ECO:0000313|Proteomes:UP000007796};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..663
FT /note="Endoplasmic reticulum chaperone BiP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003262026"
SQ SEQUENCE 663 AA; 72475 MW; 0515E0437B942D60 CRC64;
MASSWRGPKF GLGLALVTLF CLLFSPAFVG QVRADEVQEY GTVIGIDLGT TYSCVGVMQK
GKVEILVNDQ GHRITPSYVA FTEEERLVGD AAKNQAASNP EKTIFDIKRL IGRKFSEKDV
QTDIKHFPYK VVSKADKPVV KVDVKGEEKT FSPEEISGMI LGKMKEVAEG YLGKKVTHAV
VTVPAYFNDN QRQATKDAGT IAGLNVLRIV NEPTAAAIAY GLDKTDGERQ IIVYDLGGGT
FDVSLLSIDQ GVFEVLATAG DTHLGGEDFD QRIINHFAKQ FNKKNSVDVT SDKKAMGKLK
REAEKAKRTL SSQMSTRIEI ESFFGGEDFS ETLTRAKFEE LNLDLFKKTL KPVEQVLKDA
KVSKSEIDDI VLVGGSTRIP KVISLLEEFF GGKKASKGIN PDEAVAFGAA VQAGVLSGEE
GTEEIVLMDV NPLTLGIETT GGVMTKLINR NTPIPTRKSQ IFSTAADNQP VVLIQVFEGE
RSMTKDNNIL GKFELTGIPP APRGVPQIEV SFELDANGIL KVSAHDKGTG KSESITINND
KGRLTQDEID RMVAEAEKYA EEDKATRERI EARNGLENYA FSLKNQVSDE DGLGGKISEE
DKETLIEAVK ETQEWLDENA ATADTEDFEE QKEKLSNVAY PITSKMYSQA GGDDDEPSGH
DEL
//
