SOFIC_SHEON
ID SOFIC_SHEON Reviewed; 372 AA.
AC Q8E9K5;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein adenylyltransferase SoFic;
DE EC=2.7.7.n1 {ECO:0000269|PubMed:23738009};
DE AltName: Full=AMPylator SoFic;
GN Name=fic; OrderedLocusNames=SO_4266;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-73.
RC STRAIN=MR-1;
RX PubMed=22266942; DOI=10.1038/nature10729;
RA Engel P., Goepfert A., Stanger F.V., Harms A., Schmidt A., Schirmer T.,
RA Dehio C.;
RT "Adenylylation control by intra- or intermolecular active-site obstruction
RT in Fic proteins.";
RL Nature 482:107-110(2012).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), AND SUBUNIT.
RC STRAIN=MR-1;
RX PubMed=19127588; DOI=10.1002/prot.22338;
RA Das D., Krishna S.S., McMullan D., Miller M.D., Xu Q., Abdubek P.,
RA Acosta C., Astakhova T., Axelrod H.L., Burra P., Carlton D., Chiu H.J.,
RA Clayton T., Deller M.C., Duan L., Elias Y., Elsliger M.A., Ernst D.,
RA Feuerhelm J., Grzechnik A., Grzechnik S.K., Hale J., Han G.W.,
RA Jaroszewski L., Jin K.K., Klock H.E., Knuth M.W., Kozbial P., Kumar A.,
RA Marciano D., Morse A.T., Murphy K.D., Nigoghossian E., Okach L.,
RA Oommachen S., Paulsen J., Reyes R., Rife C.L., Sefcovic N., Tien H.,
RA Trame C.B., Trout C.V., van den Bedem H., Weekes D., White A.,
RA Hodgson K.O., Wooley J., Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.;
RT "Crystal structure of the Fic (Filamentation induced by cAMP) family
RT protein SO4266 (gi|24375750) from Shewanella oneidensis MR-1 at 1.6 A
RT resolution.";
RL Proteins 75:264-271(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 2-372 OF WILD-TYPE AND MUTANT
RP GLU-73 IN COMPLEXES WITH ATP; ATP ANALOG AND MAGNESIUM, CATALYTIC ACTIVITY,
RP AND MUTAGENESIS OF GLU-73.
RX PubMed=23738009; DOI=10.1371/journal.pone.0064901;
RA Goepfert A., Stanger F.V., Dehio C., Schirmer T.;
RT "Conserved inhibitory mechanism and competent ATP binding mode for
RT adenylyltransferases with Fic fold.";
RL PLoS ONE 8:E64901-E64901(2013).
CC -!- FUNCTION: Adenylyltransferase that mediates the addition of adenosine
CC 5'-monophosphate (AMP) to specific residues of target proteins.
CC {ECO:0000269|PubMed:22266942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-
CC tyrosyl-[protein]; Xref=Rhea:RHEA:54288, Rhea:RHEA-COMP:10136,
CC Rhea:RHEA-COMP:13846, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:83624; EC=2.7.7.n1;
CC Evidence={ECO:0000269|PubMed:23738009};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = 3-O-(5'-adenylyl)-L-threonyl-
CC [protein] + diphosphate; Xref=Rhea:RHEA:54292, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:13847, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138113; EC=2.7.7.n1;
CC Evidence={ECO:0000269|PubMed:23738009};
CC -!- ACTIVITY REGULATION: Adenylyltransferase activity is inhibited by the
CC inhibitory helix present at the N-terminus: Glu-73 binds ATP and
CC competes with ATP-binding at Arg-209, thereby preventing
CC adenylyltransferase activity. Activation dissociates ATP-binding from
CC Glu-73, allowing ordered binding of the entire ATP moiety with the
CC alpha-phosphate in an orientation that is productive for accepting an
CC incoming target hydroxyl side chain. {ECO:0000269|PubMed:22266942}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19127588}.
CC -!- MISCELLANEOUS: Defined as class II fido-domain containing proteins, in
CC which the inhibitory helix is present at the N-terminus of the Fido
CC domain. {ECO:0000305|PubMed:22266942}.
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DR EMBL; AE014299; AAN57237.1; -; Genomic_DNA.
DR RefSeq; NP_719793.1; NC_004347.2.
DR RefSeq; WP_011073937.1; NZ_CP053946.1.
DR PDB; 3EQX; X-ray; 1.60 A; A/B=1-372.
DR PDB; 3ZCN; X-ray; 1.70 A; A/B=2-372.
DR PDB; 3ZEC; X-ray; 2.20 A; A/B=2-372.
DR PDBsum; 3EQX; -.
DR PDBsum; 3ZCN; -.
DR PDBsum; 3ZEC; -.
DR AlphaFoldDB; Q8E9K5; -.
DR SMR; Q8E9K5; -.
DR DIP; DIP-60139N; -.
DR STRING; 211586.SO_4266; -.
DR PaxDb; Q8E9K5; -.
DR DNASU; 1171869; -.
DR KEGG; son:SO_4266; -.
DR PATRIC; fig|211586.12.peg.4125; -.
DR eggNOG; COG3177; Bacteria.
DR HOGENOM; CLU_047250_1_1_6; -.
DR OMA; ISTRLFK; -.
DR OrthoDB; 1232677at2; -.
DR PhylomeDB; Q8E9K5; -.
DR BioCyc; SONE211586:G1GMP-3941-MON; -.
DR BRENDA; 2.7.7.B23; 5706.
DR EvolutionaryTrace; Q8E9K5; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
DR Gene3D; 1.10.3290.10; -; 1.
DR InterPro; IPR025758; Fic/DOC_N.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR InterPro; IPR040198; Fido_containing.
DR InterPro; IPR026287; SoFic-like.
DR PANTHER; PTHR13504; PTHR13504; 1.
DR Pfam; PF02661; Fic; 1.
DR Pfam; PF13784; Fic_N; 1.
DR PIRSF; PIRSF038925; AMP-prot_trans; 1.
DR SUPFAM; SSF140931; SSF140931; 1.
DR PROSITE; PS51459; FIDO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..372
FT /note="Protein adenylyltransferase SoFic"
FT /id="PRO_0000417548"
FT DOMAIN 121..262
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT MOTIF 69..74
FT /note="Inhibitory (S/T)XXXE(G/N) motif"
FT BINDING 73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 203..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 73
FT /note="E->G: Promotes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22266942,
FT ECO:0000269|PubMed:23738009"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 28..50
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 54..72
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 94..112
FT /evidence="ECO:0007829|PDB:3EQX"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 120..131
FT /evidence="ECO:0007829|PDB:3EQX"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3EQX"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 183..197
FT /evidence="ECO:0007829|PDB:3EQX"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:3EQX"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 253..292
FT /evidence="ECO:0007829|PDB:3EQX"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:3EQX"
FT STRAND 309..312
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:3EQX"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 324..336
FT /evidence="ECO:0007829|PDB:3EQX"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:3EQX"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:3ZEC"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3EQX"
FT HELIX 354..361
FT /evidence="ECO:0007829|PDB:3EQX"
SQ SEQUENCE 372 AA; 42225 MW; FFEF7D98ACD2C74D CRC64;
MEWQAEQAYN HLPPLPLDSK LAELAETLPI LKACIPARAA LAELKQAGEL LPNQGLLINL
LPLLEAQGSS EIENIVTTTD KLFQYAQEDS QADPMTKEAL RYRTALYQGF TQLSNRPLCV
TTALEICSTI KSVQMDVRKV PGTSLTNQAT GEVIYTPPAG ESVIRDLLSN WEAFLHNQDD
VDPLIKMAMA HYQFEAIHPF IDGNGRTGRV LNILYLIDQQ LLSAPILYLS RYIVAHKQDY
YRLLLNVTTQ QEWQPWIIFI LNAVEQTAKW TTHKIAAARE LIAHTTEYVR QQLPKIYSHE
LVQVIFEQPY CRIQNLVESG LAKRQTASVY LKQLCDIGVL EEVQSGKEKL FVHPKFVTLM
TKDSNQFSRY AL
