ID F9FL45_FUSOF Unreviewed; 663 AA.
AC F9FL45;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=FOXB_07124 {ECO:0000313|EMBL:EGU82295.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU82295.1};
RN [1] {ECO:0000313|EMBL:EGU82295.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU82295.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU82295.1}.
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DR EMBL; AFQF01002161; EGU82295.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FL45; -.
DR STRING; 660025.F9FL45; -.
DR PaxDb; 5507-FOXG_06163P0; -.
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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..663
FT /note="Endoplasmic reticulum chaperone BiP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003383152"
SQ SEQUENCE 663 AA; 72593 MW; 598EBDA7C9973BBB CRC64;
MARSRSSMAL GLGLLCWIAL LFSPLAFVQT VQADEVDNYG TVIGIDLGTT YSCVGVMQKG
KVEILVNDQG NRITPSYVAF TEDERLVGDA AKNQAAANPT NTIYDIKRLI GRKYSEKTLQ
GDIKHFPFKV VNRDDRPVVQ VEVDGAKKQF TPEEISAMVL GKMKEVAEGY LGKKVTHAVV
TVPAYFNDNQ RQATKDAGII AGLNVLRIVN EPTAAAIAYG LDKTDGERQI IVYDLGGGTF
DVSLLSIDDG IFEVLATAGD THLGGEDFDQ RVINYFAKQY NQKNNVDITK DLKAMGKLKR
EAEKAKRTLS SQKSTRIEIE AFHNGKDFSE TLTQAKFEEL NIDLFKKTMK PVEQVLKDAK
LKKSDVDDIV LVGGSTRIPK VQQLIEDFFN KKASKGINPD EAVAFGAAVQ AGVLSGEEGT
SGVVLMDVNP LTLGIETTGG VMTKLIPRNT AIPTRKSQIF STAADNQPVV LIQVFEGERS
LTKDNNILGK FELTGIPPAP RGVPQIEVSF ELDANGILKV SAHDKGTGKQ ESITITNDKG
RLTPEEIERM VAEAEKYAEE DKATRERIEA RNGLENYAFS LKNQVNDEEG LGGKIEEDDK
ETILEAVKET NEWLDEHGAD ATAEDFEEQK EKLSNVAYPI TSKMYQSAGG AGGEQDDNIH
DEL
//
