NMFIC_NEIMB
ID NMFIC_NEIMB Reviewed; 191 AA.
AC Q7DDR9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein adenylyltransferase NmFic;
DE EC=2.7.7.n1 {ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:23738009};
DE AltName: Full=AMPylator NmFic;
GN OrderedLocusNames=NMB0255;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
RA Cuff M.E., Bigelow L., Bargassa M., Joachimiak A.;
RT "Structure of a putative cell filamentation protein from Neisseria
RT meningitidis.";
RL Submitted (FEB-2006) to the PDB data bank.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 11-167 IN COMPLEX WITH ATP,
RP CATALYTIC ACTIVITY, FUNCTION, AMPYLATION AT TYR-183, ACTIVITY REGULATION,
RP AND MUTAGENESIS OF SER-182 AND GLU-186.
RC STRAIN=MC58;
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 11-191 OF MUTANT GLY-186 IN
RP COMPLEX WITH ATP ANALOG, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF
RP GLU-186.
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:22266942, 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:22266942, ECO:0000269|PubMed:23738009};
CC -!- ACTIVITY REGULATION: Adenylyltransferase activity is inhibited by the
CC inhibitory helix present at the C-terminus: Glu-186 binds ATP and
CC competes with ATP-binding at Arg-118, thereby preventing
CC adenylyltransferase activity. Activation dissociates ATP-binding from
CC Glu-186, 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:22266942,
CC ECO:0000269|PubMed:23738009}.
CC -!- PTM: Auto-AMPylation at Tyr-183 in vitro.
CC {ECO:0000269|PubMed:22266942}.
CC -!- MISCELLANEOUS: Defined as class III fido-domain containing proteins, in
CC which the inhibitory helix is present at the C-terminus of the Fido
CC domain. {ECO:0000305|PubMed:22266942}.
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DR EMBL; AE002098; AAF40709.1; -; Genomic_DNA.
DR PIR; B81220; B81220.
DR RefSeq; NP_273311.1; NC_003112.2.
DR RefSeq; WP_002215631.1; NC_003112.2.
DR PDB; 2G03; X-ray; 2.20 A; A=1-191.
DR PDB; 3S6A; X-ray; 2.20 A; A=11-191.
DR PDB; 3SE5; X-ray; 1.70 A; A/B/C/D=11-167.
DR PDB; 3SN9; X-ray; 3.03 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=11-191.
DR PDB; 3ZLM; X-ray; 2.00 A; A=11-191.
DR PDB; 5CGL; X-ray; 2.35 A; A/B=11-191.
DR PDB; 5CKL; X-ray; 0.99 A; A=11-191.
DR PDB; 5CMT; X-ray; 0.99 A; A=11-191.
DR PDBsum; 2G03; -.
DR PDBsum; 3S6A; -.
DR PDBsum; 3SE5; -.
DR PDBsum; 3SN9; -.
DR PDBsum; 3ZLM; -.
DR PDBsum; 5CGL; -.
DR PDBsum; 5CKL; -.
DR PDBsum; 5CMT; -.
DR AlphaFoldDB; Q7DDR9; -.
DR SMR; Q7DDR9; -.
DR DIP; DIP-60138N; -.
DR STRING; 122586.NMB0255; -.
DR PaxDb; Q7DDR9; -.
DR EnsemblBacteria; AAF40709; AAF40709; NMB0255.
DR KEGG; nme:NMB0255; -.
DR PATRIC; fig|122586.8.peg.318; -.
DR HOGENOM; CLU_080158_4_0_4; -.
DR OMA; GHFRFAN; -.
DR EvolutionaryTrace; Q7DDR9; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005524; F:ATP 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 GO; GO:0051302; P:regulation of cell division; IBA:GO_Central.
DR Gene3D; 1.10.3290.10; -; 1.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR Pfam; PF02661; Fic; 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 Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..191
FT /note="Protein adenylyltransferase NmFic"
FT /id="PRO_0000417551"
FT DOMAIN 37..162
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT MOTIF 182..187
FT /note="Inhibitory (S/T)XXXE(G/N) motif"
FT BINDING 67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22266942"
FT BINDING 104..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22266942"
FT BINDING 112..118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22266942"
FT BINDING 140..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22266942"
FT BINDING 186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22266942"
FT MOD_RES 183
FT /note="O-AMP-tyrosine; in vitro"
FT /evidence="ECO:0000269|PubMed:22266942"
FT MUTAGEN 182
FT /note="S->A: Promotes adenylyltransferase activity; when
FT associated with A-186."
FT /evidence="ECO:0000269|PubMed:22266942"
FT MUTAGEN 186
FT /note="E->A: Promotes adenylyltransferase activity; when
FT associated with A-182."
FT /evidence="ECO:0000269|PubMed:22266942,
FT ECO:0000269|PubMed:23738009"
FT MUTAGEN 186
FT /note="E->G: Promotes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22266942,
FT ECO:0000269|PubMed:23738009"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:5CKL"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:5CKL"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:5CKL"
FT HELIX 39..50
FT /evidence="ECO:0007829|PDB:5CKL"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:5CKL"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:5CKL"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:5CKL"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:5CKL"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5CKL"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:5CKL"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5CKL"
FT HELIX 140..149
FT /evidence="ECO:0007829|PDB:5CKL"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:5CKL"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:5CKL"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:5CKL"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:5CKL"
SQ SEQUENCE 191 AA; 22190 MW; DAE3849D07424543 CRC64;
MPSENPIGKT MKSIDEQSLH NARRLFESGD IDRIEVGTTA GLQQIHRYLF GGLYDFAGQI
REDNISKGGF RFANAMYLKE ALVKIEQMPE RTFEEIIAKY VEMNIAHPFL EGNGRSTRIW
LDLVLKKNLK KVVNWQNVSK TLYLQAMERS PVNDLELRFL LKDNLTDDVD NREIIFKGIE
QSYYYEGYEK G
