ID A0A084QHZ8_STAC4 Unreviewed; 662 AA.
AC A0A084QHZ8;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=S40285_04115 {ECO:0000313|EMBL:KFA63583.1};
OS Stachybotrys chlorohalonata (strain IBT 40285).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA63583.1, ECO:0000313|Proteomes:UP000028524};
RN [1] {ECO:0000313|EMBL:KFA63583.1, ECO:0000313|Proteomes:UP000028524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA63583.1,
RC ECO:0000313|Proteomes:UP000028524};
RX PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT the toxigenic black mold Stachybotrys.";
RL BMC Genomics 15:590-590(2014).
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; KL660735; KFA63583.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A084QHZ8; -.
DR STRING; 1283841.A0A084QHZ8; -.
DR HOGENOM; CLU_005965_7_0_1; -.
DR InParanoid; A0A084QHZ8; -.
DR OMA; AYTKNQD; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000028524; 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:UP000028524};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..662
FT /note="Endoplasmic reticulum chaperone BiP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001779264"
SQ SEQUENCE 662 AA; 72360 MW; 4660160DB4F15A3F CRC64;
MAQSRSSLAL GLGLLCWITL LFSPLAFVQT VNADDSENYG TVIGIDLGTT YSCVGVMQKG
KVEILVNDQG NRITPSYVAF TEDERLVGDS AKNQAAANPY NTIFDVKRLI GRKFNEKEVQ
ADIKHFPYKV ISKDGKPLVQ VEVSGENKNF TPEEISAMIL GKMKEVAESY LGKKVTHAVV
TVPAYFNDNQ RQATKDAGII AGLNVLRIVN EPTAAAIAYG LDRTSEERQI IVYDLGGGTF
DVSLLSLDHG VFEVLATAGD THLGGEDFDQ RLINHFAKTY NKAHGVDVTK NAKAMGKLKR
EAEKAKRTLS SQTSTRIEIE AFFEGNDFSE SLTRAKFEEL NIDLFKKTLK PVEQVLKDAK
VSKSEVDDIV LVGGSTRIPK VQELIEEYFN GKKASKGINP DEAVAFGAAV QAGILSGEEG
TDDIVLMDVN PLTLGIETTG GVMTKLIPRN TAIPTRKAQI FSTAADNQPV VLIQVFEGER
SMTKDNNLLG KFELTGIPPA PRGVPQIEVT FELDANGILK VSAHDKGTGK SESVTINNDK
GRLSQEEIDR MVAEAEQYAE EDKATRERIE ARNGLENYAF SLKNQVNDEE GLGGKIDDDD
KETILDAVKE ATEWLEENGA EATTEDFEEQ KEKLSNVAYP ITSKMYQGAG GDDDSGDFKD
EL
//
