ID C1GRW7_PARBA Unreviewed; 677 AA.
AC C1GRW7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 2.
DT 27-MAR-2024, entry version 71.
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=PAAG_01262 {ECO:0000313|EMBL:EEH38342.2};
OS Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS brasiliensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502779 {ECO:0000313|EMBL:EEH38342.2, ECO:0000313|Proteomes:UP000002059};
RN [1] {ECO:0000313|EMBL:EEH38342.2, ECO:0000313|Proteomes:UP000002059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-826 / Pb01 {ECO:0000313|Proteomes:UP000002059};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(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; KN293993; EEH38342.2; -; Genomic_DNA.
DR RefSeq; XP_015701070.1; XM_015844289.1.
DR AlphaFoldDB; C1GRW7; -.
DR STRING; 502779.C1GRW7; -.
DR GeneID; 9100141; -.
DR KEGG; pbl:PAAG_01262; -.
DR VEuPathDB; FungiDB:PAAG_01262; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_7_0_1; -.
DR OMA; AYTKNQD; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000002059; Partially assembled 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:UP000002059};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..677
FT /note="Endoplasmic reticulum chaperone BiP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002908512"
FT REGION 653..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 677 AA; 73835 MW; E7345485376E0277 CRC64;
MSRMSRRDAS SSPFAWTTVL YLLLVFIAPL ALLGTAHAEG DQAPLKEDYG TVIGIDLGTT
YSCVGAMQNG KVEIFVNDQG NRITPSYVAF TDDERLVGDA AKNQYAANPQ RTIFDIKRLI
GRKFDDQDAQ KDIKHFPFRV VNKDGKPQVK VEVNGKDKTF TPEEVSAMIL GKMKEVAENY
LGKTVTNAVV TVPAYFNDNQ RQATKDAGTI AGLNVLRVVN EPTAAAIAYG LDKTGDERQI
IVYDLGGGTF DVSLLSIDNG AFEVLATAGD THLGGEDFDQ RVISHFVKQY NKKHNVDITK
DLKTMGKLKR EVEKAKRTLS SQMSTRIEIE AFHDGKDFSE TLTRAKFEEL NMDLFKKTLR
PVEQVLKDAK VKKSEIHDIV LVGGSTRIPK VQALLEEFFG GKKASKGINP DEAVAFGAAI
QGGVLSGDEG ASEIVLMDVN PLTLGIETTG GIMTKLIPRN TVIPTRKSQI FSTAADNQPV
VLIQVYEGER PLTKDNNLLG KFELTGIPPA PRGVPQIEVS FELDANGILK VTAGDKGTGK
AESITITNDK GRLSQEEIDR MVAEAAEFAE EDKAMKAKID ARNTLENYAF SLKNQVQDEE
GLGGKIDKDD KETILEAVKE TTDWLEENAA KATTEDFEEQ KEKLSNVAYP ITSKLYSGGA
GGAPGGDDDE PSGHDEL
//
