ID K1WW58_MARBU Unreviewed; 671 AA.
AC K1WW58;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=MBM_05151 {ECO:0000313|EMBL:EKD16682.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD16682.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD16682.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD16682.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(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}.
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DR EMBL; JH921438; EKD16682.1; -; Genomic_DNA.
DR RefSeq; XP_007293040.1; XM_007292978.1.
DR AlphaFoldDB; K1WW58; -.
DR STRING; 1072389.K1WW58; -.
DR GeneID; 18761086; -.
DR KEGG; mbe:MBM_05151; -.
DR eggNOG; KOG0100; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; K1WW58; -.
DR OMA; AYTKNQD; -.
DR OrthoDB; 143at2759; -.
DR Proteomes; UP000006753; 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:UP000006753};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..671
FT /note="Endoplasmic reticulum chaperone BiP"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003852759"
FT REGION 651..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 671 AA; 73319 MW; ECB578B2F5524160 CRC64;
MARGNTSSTW MGLSALFYLS LLFAPLALVG RVNAEAEQEP LQENYGTVIG IDLGTTYSCV
GVMQKGKVEI LVNDQGHRIT PSYVAFTDDE RLVGDAAKNQ AAANPTNTIF DIKRMIGRKF
SDKDVQGDMK HFPFNVVEKD GKPHVKVQVS GAPKTFTPEE ISAMILGKMK DVAESYLGNK
VTHAVVTVPA YFNDNQRQAT KDAGIIAGLN VLRIVNEPTA AAIAYGLDKT EGERQIIVYD
LGGGTFDVSL LSIDRGVFEV LSTAGDTHLG GEDFDQRVIN YFAKKYNKDN NVDITKDLKT
MGKLKREAEK AKRTLSSQKT TRIEIEAFHN GNDFSETLTR AKFEELNIDL FRKTLKPVEQ
VLKDAKIKKA EVDDIVLVGG STRIPKVVEL IEEYFGGKKA SKGINPDEAV AFGAAVQGGV
LSGEEGTEEL VLMDVNPLTL GIETTGGVMT KLIPRNTVIP TRKSQIFSTA ADNQPVVLIQ
VFEGERTMTK DNNNLGKFEL TGIPAAPRGV PQIEVSFELD ANGILKVSAS DKGTGKVESI
TITNDKGRLT QEEIDRMVQE AEKYADEDKA TKERIEARNG LENYAFSLKN QVNDEEGLGG
KIEENDKETL LEAIKETTDW LEENSATANA EDFEEQKEKL SNVAYPITSK LYDGAGGPAG
GDDEPDSHDE L
//
