BIP_CRIGR
ID BIP_CRIGR Reviewed; 654 AA.
AC G3I8R9;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Endoplasmic reticulum chaperone BiP {ECO:0000250|UniProtKB:P11021};
DE EC=3.6.4.10 {ECO:0000269|PubMed:29198525};
DE AltName: Full=78 kDa glucose-regulated protein {ECO:0000250|UniProtKB:P11021};
DE Short=GRP-78 {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=Binding-immunoglobulin protein {ECO:0000303|PubMed:29198525};
DE Short=BiP {ECO:0000303|PubMed:29198525};
DE AltName: Full=Heat shock protein 70 family protein 5 {ECO:0000250|UniProtKB:P11021};
DE Short=HSP70 family protein 5 {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=Heat shock protein family A member 5 {ECO:0000250|UniProtKB:P11021};
DE AltName: Full=Immunoglobulin heavy chain-binding protein {ECO:0000303|PubMed:29198525};
DE Flags: Precursor;
GN Name=HSPA5 {ECO:0000250|UniProtKB:P11021};
GN Synonyms=GRP78 {ECO:0000250|UniProtKB:P11021};
GN ORFNames=I79_019946 {ECO:0000312|EMBL:EGV94255.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
RN [2]
RP SUBUNIT, ACTIVITY REGULATION, DOMAIN, AND MUTAGENESIS OF THR-229;
RP 414-LEU--LEU-417 AND VAL-461.
RX PubMed=26473973; DOI=10.7554/elife.08961;
RA Preissler S., Chambers J.E., Crespillo-Casado A., Avezov E., Miranda E.,
RA Perez J., Hendershot L.M., Harding H.P., Ron D.;
RT "Physiological modulation of BiP activity by trans-protomer engagement of
RT the interdomain linker.";
RL Elife 4:E08961-E08961(2015).
RN [3]
RP AMPYLATION AT THR-518, AND MUTAGENESIS OF THR-518; THR-525 AND THR-527.
RX PubMed=26673894; DOI=10.7554/elife.12621;
RA Preissler S., Rato C., Chen R., Antrobus R., Ding S., Fearnley I.M.,
RA Ron D.;
RT "AMPylation matches BiP activity to client protein load in the endoplasmic
RT reticulum.";
RL Elife 4:E12621-E12621(2015).
RN [4]
RP FUNCTION, INTERACTION WITH ERN1, AND MUTAGENESIS OF THR-229 AND VAL-461.
RX PubMed=29198525; DOI=10.1016/j.cell.2017.10.040;
RA Amin-Wetzel N., Saunders R.A., Kamphuis M.J., Rato C., Preissler S.,
RA Harding H.P., Ron D.;
RT "A J-Protein co-chaperone recruits bip to monomerize IRE1 and repress the
RT unfolded protein response.";
RL Cell 171:1625-1637(2017).
RN [5]
RP AMPYLATION AT THR-518.
RX PubMed=29064369; DOI=10.7554/elife.29430;
RA Wieteska L., Shahidi S., Zhuravleva A.;
RT "Allosteric fine-tuning of the conformational equilibrium poises the
RT chaperone BiP for post-translational regulation.";
RL Elife 6:0-0(2017).
RN [6]
RP AMPYLATION AT THR-518, AND DEAMPYLATION AT THR-518.
RX PubMed=27918543; DOI=10.1038/nsmb.3337;
RA Preissler S., Rato C., Perera L., Saudek V., Ron D.;
RT "FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic
RT reticulum chaperone BiP.";
RL Nat. Struct. Mol. Biol. 24:23-29(2017).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 28-549 IN COMPLEX WITH ADP,
RP ACTIVITY REGULATION, AMPYLATION AT THR-518, AND MUTAGENESIS OF THR-229 AND
RP VAL-461.
RX PubMed=29064368; DOI=10.7554/elife.29428;
RA Preissler S., Rohland L., Yan Y., Chen R., Read R.J., Ron D.;
RT "AMPylation targets the rate-limiting step of BiP's ATPase cycle for its
RT functional inactivation.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Endoplasmic reticulum chaperone that plays a key role in
CC protein folding and quality control in the endoplasmic reticulum lumen
CC (By similarity). Involved in the correct folding of proteins and
CC degradation of misfolded proteins via its interaction with
CC DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from
CC its substrate (By similarity). Acts as a key repressor of the
CC ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:29198525).
CC In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to
CC the luminal region of ERN1/IRE1, leading to disrupt the dimerization of
CC ERN1/IRE1, thereby inactivating ERN1/IRE1 (PubMed:29198525).
CC Accumulation of misfolded protein in the endoplasmic reticulum causes
CC release of HSPA5/BiP from ERN1/IRE1, allowing homodimerization and
CC subsequent activation of ERN1/IRE1 (PubMed:29198525). Plays an
CC auxiliary role in post-translational transport of small presecretory
CC proteins across endoplasmic reticulum (ER). May function as an
CC allosteric modulator for SEC61 channel-forming translocon complex,
CC likely cooperating with SEC62 to enable the productive insertion of
CC these precursors into SEC61 channel. Appears to specifically regulate
CC translocation of precursors having inhibitory residues in their mature
CC region that weaken channel gating. May also play a role in apoptosis
CC and cell proliferation (By similarity). {ECO:0000250|UniProtKB:P11021,
CC ECO:0000250|UniProtKB:P20029, ECO:0000269|PubMed:29198525}.
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:0000269|PubMed:29198525};
CC -!- ACTIVITY REGULATION: The chaperone activity is regulated by ATP-induced
CC allosteric coupling of the nucleotide-binding (NBD) and substrate-
CC binding (SBD) domains (By similarity). In the ADP-bound and nucleotide-
CC free (apo) states, the two domains have little interaction (By
CC similarity). In contrast, in the ATP-bound state the two domains are
CC tightly coupled, which results in drastically accelerated kinetics in
CC both binding and release of polypeptide substrates (By similarity). J
CC domain-containing co-chaperones (DNAJB9/ERdj4 or DNAJC10/ERdj5)
CC stimulate the ATPase activity and are required for efficient substrate
CC recognition by HSPA5/BiP (PubMed:29064368). Homooligomerization
CC inactivates participating HSPA5/BiP protomers and probably act as
CC reservoirs to store HSPA5/BiP molecules when they are not needed by the
CC cell (PubMed:26473973). {ECO:0000250|UniProtKB:P11021,
CC ECO:0000269|PubMed:26473973, ECO:0000269|PubMed:29064368}.
CC -!- SUBUNIT: Monomer and homooligomer; homooligomerization via the
CC interdomain linker inactivates the chaperone activity and acts as a
CC storage of HSPA5/BiP molecules (PubMed:26473973). Interacts with DNAJC1
CC (via J domain) (By similarity). Component of an EIF2 complex at least
CC composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and
CC HSPA5 (By similarity). Part of a large chaperone multiprotein complex
CC comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB,
CC SDF2L1, UGGT1 and very small amounts of ERP29, but not, or at very low
CC levels, CALR nor CANX (By similarity). Interacts with TMEM132A and
CC TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1. Interacts
CC with DNAJC10 (By similarity). Interacts with DNAJB9/ERdj4; leading to
CC recruit HSPA5/BiP to ERN1/IRE1 (PubMed:29198525). Interacts with
CC ERN1/IRE1; interaction takes place following interaction with
CC DNAJB9/ERdj4 and leads to inactivate ERN1/IRE1 (PubMed:29198525).
CC Interacts with MX1 (By similarity). Interacts with METTL23. Interacts
CC with CEMIP; the interaction induces calcium leakage from the
CC endoplasmic reticulum and cell migration. Interacts with PCSK4 form;
CC the interaction takes place in the endoplasmic reticulum. Interacts
CC with CIPC. Interacts with CCDC88B (via C-terminus); the interaction
CC opposes ERN1-mediated JNK activation, protecting against apoptosis.
CC Interacts with INPP5K; necessary for INPP5K localization at the
CC endoplasmic reticulum. Interacts with LOXL2; leading to activate the
CC ERN1/IRE1-XBP1 pathway of the unfolded protein response (By
CC similarity). Interacts with CLU under stressed condition; interaction
CC increases CLU protein stability; facilitates its retrotranslocation and
CC redistribution to the mitochondria; cooperatively suppress stress-
CC induced apoptosis by stabilizing mitochondrial membrane integrity (By
CC similarity). Interacts with CCDC47 (By similarity). Interacts with CLN3
CC (By similarity). Interacts with KIAA1324; may regulate the function of
CC HSPA5 in apoptosis and cell proliferation. Interacts with CASP7 (By
CC similarity). Interacts with ILDR2; the interaction stabilizes ILDR2
CC expression (By similarity). {ECO:0000250|UniProtKB:P11021,
CC ECO:0000250|UniProtKB:P20029, ECO:0000269|PubMed:26473973,
CC ECO:0000269|PubMed:29198525}.
CC -!- INTERACTION:
CC G3I8R9; A0A3L7I3A5: CgPICR_003176; NbExp=3; IntAct=EBI-988311, EBI-1557743;
CC G3I8R9; G3IL63: I79_024625; NbExp=3; IntAct=EBI-988311, EBI-6429131;
CC G3I8R9; O55242: Sigmar1; Xeno; NbExp=3; IntAct=EBI-988311, EBI-1557700;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:P11021}. Melanosome
CC {ECO:0000250|UniProtKB:P11021}. Cytoplasm
CC {ECO:0000250|UniProtKB:P20029}. Cell surface. Note=Identified by mass
CC spectrometry in melanosome fractions from stage I to stage IV (By
CC similarity). Localizes to the cell surface in epithelial cells; high
CC levels of free iron promotes cell surface localization (By similarity).
CC {ECO:0000250|UniProtKB:P11021}.
CC -!- DOMAIN: The interdomain linker regulates the chaperone activity by
CC mediating the formation of homooligomers. Homooligomers are formed by
CC engagement of the interdomain linker of one HSPA5/BiP molecule as a
CC typical substrate of an adjacent HSPA5/BiP molecule. HSPA5/BiP
CC oligomerization inactivates participating HSPA5/BiP protomers.
CC HSPA5/BiP oligomers probably act as reservoirs to store HSPA5/BiP
CC molecules when they are not needed by the cell. When the levels of
CC unfolded proteins rise, cells can rapidly break up these oligomers to
CC make active monomers. {ECO:0000269|PubMed:26473973}.
CC -!- PTM: In unstressed cells, AMPylation at Thr-518 by FICD inactivates the
CC chaperome activity: AMPylated form is locked in a relatively inert
CC state and only weakly stimulated by J domain-containing proteins
CC (PubMed:26673894, PubMed:29198525, PubMed:29064369, PubMed:27918543).
CC In response to endoplasmic reticulum stress, de-AMPylation by the same
CC protein, FICD, restores the chaperone activity (PubMed:27918543).
CC {ECO:0000269|PubMed:26673894, ECO:0000269|PubMed:27918543,
CC ECO:0000269|PubMed:29064369, ECO:0000269|PubMed:29198525}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; JH001529; EGV94255.1; -; Genomic_DNA.
DR RefSeq; NP_001233668.1; NM_001246739.2.
DR PDB; 5O4P; X-ray; 1.86 A; A/B=28-549.
DR PDB; 6EOB; X-ray; 2.00 A; A=28-549.
DR PDB; 6EOC; X-ray; 1.67 A; A=28-549.
DR PDB; 6EOE; X-ray; 1.71 A; A=28-549.
DR PDB; 6EOF; X-ray; 1.59 A; A=28-549.
DR PDB; 6H9U; X-ray; 1.57 A; A=28-413.
DR PDB; 6HA7; X-ray; 2.49 A; A/B=28-413.
DR PDB; 6HAB; X-ray; 2.08 A; A=28-549.
DR PDB; 6ZYH; X-ray; 1.88 A; A/B=28-406.
DR PDB; 7A4U; X-ray; 1.77 A; A=28-549.
DR PDB; 7A4V; X-ray; 1.94 A; A=28-549.
DR PDB; 7B7Z; X-ray; 1.70 A; B=28-549.
DR PDB; 7B80; X-ray; 1.87 A; B=28-549.
DR PDBsum; 5O4P; -.
DR PDBsum; 6EOB; -.
DR PDBsum; 6EOC; -.
DR PDBsum; 6EOE; -.
DR PDBsum; 6EOF; -.
DR PDBsum; 6H9U; -.
DR PDBsum; 6HA7; -.
DR PDBsum; 6HAB; -.
DR PDBsum; 6ZYH; -.
DR PDBsum; 7A4U; -.
DR PDBsum; 7A4V; -.
DR PDBsum; 7B7Z; -.
DR PDBsum; 7B80; -.
DR AlphaFoldDB; G3I8R9; -.
DR SMR; G3I8R9; -.
DR IntAct; G3I8R9; 6.
DR STRING; 10029.NP_001233668.1; -.
DR GeneID; 100689305; -.
DR KEGG; cge:100689305; -.
DR CTD; 3309; -.
DR eggNOG; KOG0100; Eukaryota.
DR InParanoid; G3I8R9; -.
DR OMA; AYTKNQD; -.
DR OrthoDB; 288077at2759; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:1903895; P:negative regulation of IRE1-mediated unfolded protein response; IDA:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IDA:GO_Central.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISS:UniProtKB.
DR CDD; cd10241; HSPA5-like_NBD; 1.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
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; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW Endoplasmic reticulum; Hydrolase; Isopeptide bond; Methylation; Nitration;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Signal;
KW Ubl conjugation.
FT SIGNAL 1..18
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT CHAIN 19..654
FT /note="Endoplasmic reticulum chaperone BiP"
FT /id="PRO_5003445004"
FT REGION 1..80
FT /note="Required for interaction with KIAA1324"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 125..280
FT /note="Nucleotide-binding (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 409..419
FT /note="Interdomain linker"
FT /evidence="ECO:0000269|PubMed:26473973"
FT REGION 420..500
FT /note="Substrate-binding (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT REGION 632..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 651..654
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT BINDING 36..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29064368,
FT ECO:0000312|PDB:6EOE, ECO:0000312|PDB:6EOF"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT BINDING 227..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29064368,
FT ECO:0000312|PDB:6EOE, ECO:0000312|PDB:6EOF"
FT BINDING 293..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29064368,
FT ECO:0000312|PDB:6EOE, ECO:0000312|PDB:6EOF"
FT BINDING 364..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:29064368,
FT ECO:0000312|PDB:6EOE, ECO:0000312|PDB:6EOF"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06761"
FT MOD_RES 125
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 160
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 271
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 353
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 447
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 492
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 518
FT /note="O-AMP-threonine; alternate"
FT /evidence="ECO:0000269|PubMed:26673894,
FT ECO:0000269|PubMed:27918543, ECO:0000269|PubMed:29064368,
FT ECO:0000312|PDB:5O4P, ECO:0000312|PDB:6EOF"
FT MOD_RES 518
FT /note="Phosphothreonine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOD_RES 585
FT /note="N6,N6,N6-trimethyllysine; by METTL21A; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 585
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOD_RES 585
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOD_RES 591
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MOD_RES 643
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 648
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20029"
FT CROSSLNK 352
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT CROSSLNK 353
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P11021"
FT MUTAGEN 229
FT /note="T->A: Impaired ATPase activity."
FT /evidence="ECO:0000269|PubMed:26473973,
FT ECO:0000269|PubMed:29064368, ECO:0000269|PubMed:29198525"
FT MUTAGEN 414..417
FT /note="LVLL->ADDA: Abolished homooligomerization."
FT /evidence="ECO:0000269|PubMed:26473973"
FT MUTAGEN 461
FT /note="V->F: Impaired substrate-binding."
FT /evidence="ECO:0000269|PubMed:26473973,
FT ECO:0000269|PubMed:29064368, ECO:0000269|PubMed:29198525"
FT MUTAGEN 518
FT /note="T->A: Abolishes AMPylation."
FT /evidence="ECO:0000269|PubMed:26673894"
FT MUTAGEN 525
FT /note="T->A: Does not affect AMPylation."
FT /evidence="ECO:0000269|PubMed:26673894"
FT MUTAGEN 527
FT /note="T->A: Does not affect AMPylation."
FT /evidence="ECO:0000269|PubMed:26673894"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6HA7"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 78..81
FT /evidence="ECO:0007829|PDB:6H9U"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:6EOF"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6H9U"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 106..114
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 125..133
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 142..161
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 201..208
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 255..274
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 282..298
FT /evidence="ECO:0007829|PDB:6H9U"
FT TURN 299..301
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:6HA7"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 324..337
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 358..363
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 364..367
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 369..378
FT /evidence="ECO:0007829|PDB:6H9U"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:6H9U"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:6H9U"
FT HELIX 393..405
FT /evidence="ECO:0007829|PDB:6H9U"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:6EOF"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 432..437
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 442..451
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 461..472
FT /evidence="ECO:0007829|PDB:6EOF"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 476..485
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 509..515
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:6EOF"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:6EOF"
FT HELIX 535..546
FT /evidence="ECO:0007829|PDB:6EOF"
SQ SEQUENCE 654 AA; 72379 MW; 25CF665F59113A49 CRC64;
MKFPMVAAAL LLLCAVRAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR
ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV
EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ
RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG
VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS
SQHQARIEIE SFFEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV
LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC
PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG
TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER
MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE
KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTSE KDEL
