ID A0A0F7RSC2_9BASI Unreviewed; 689 AA.
AC A0A0F7RSC2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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 Name=SSCI19340.1 {ECO:0000313|EMBL:CDR99366.1};
GN ORFNames=SPSC_04015 {ECO:0000313|EMBL:CDU24514.1};
OS Sporisorium scitamineum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=49012 {ECO:0000313|EMBL:CDR99366.1, ECO:0000313|Proteomes:UP000242770};
RN [1] {ECO:0000313|EMBL:CDR99366.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman J.Paul.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDU24514.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SscI8 {ECO:0000313|EMBL:CDU24514.1};
RA Ju J., Zhang J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000242770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Berkman P.J.;
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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; CCFA01001001; CDR99366.1; -; Genomic_DNA.
DR EMBL; LK056676; CDU24514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7RSC2; -.
DR STRING; 49012.A0A0F7RSC2; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000242770; 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; 3.30.420.40; -; 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}; Signal {ECO:0000256|ARBA:ARBA00022729}.
SQ SEQUENCE 689 AA; 74553 MW; C4181B1CA471D7F6 CRC64;
MVQARRTTAL AQRRQAARAT DMSRPAFMAI IMAILALLTF SAFMAPSSSA GSMGVAAAAD
KRSEYGTVIG IDLGTTYSCV GAQVNGRVEI ITNDQGNRIT PSYVAFTPER LVGDAAKNQA
AQNPENTIFD AKRLIGRKWG ESDLKKDAKH LPFKLVEKKG KPAIQVTVNG EKKVFTPEEV
SAMVLQKMKE TAEAYLGHKV THAVVTVPAY FNDAQRQATK DAGTIAGLNV LRIVNEPTAA
AIAYGLDKKD GESQIIVYDL GGGTFDVSLL SIDSGVFEVL ATAGDTHLGG EDFDNRVSEY
ILKQFKKKTG LDASSNKRSV GKLKREVERA KRTLSSQMST KIEIDGFFEG NDLDETLTRA
KFEELNMDLF RKTMKPVEQV LKDAGVKKDE IDDVVLVGGS TRIPKVQAML KEYFGREPSK
GINPDEAVAW GAAVQGGVLA GDESLGDVVL IDVNPLTLGI ETNGGVMTKL IPRNTVVPTK
KSQIFSTAAD NQNTVLIQVF EGERSMTKDN NLLGKFELTG IPPAPRGTPQ IEVTFELDAN
GIMKVSAADK GTGKSESITI ENDKGRLTPE EIERMVAEAE EFAEQDEAVR KRIEALNNLQ
NFIASLRSQL SDKEGLGGKL DKEDKESIEQ SLKDAEAWLD ENSQTAEGSD IEEQLSELQA
AVAPITAKIY QGGAAGGNDE PLNYGHDEL
//
