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Protein

Adenosine monophosphate-protein transferase NmFic

Gene

NMB0255

Organism
Neisseria meningitidis serogroup B (strain MC58)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins.1 Publication

Catalytic activityi

ATP + [protein] = diphosphate + [protein]-AMP.2 Publications

Enzyme regulationi

Adenylyltransferase activity is inhibited by the inhibitory helix present at the C-terminus: Glu-186 binds ATP and competes with ATP-binding at Arg-118, thereby preventing adenylyltransferase activity. Activation dissociates ATP-binding from Glu-186, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei67 – 671ATP1 Publication
Binding sitei186 – 1861ATP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi104 – 1074ATP1 Publication
Nucleotide bindingi112 – 1187ATP1 Publication
Nucleotide bindingi140 – 1434ATP1 Publication

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • protein adenylyltransferase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • protein adenylylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciNMEN122586:GHGG-270-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine monophosphate-protein transferase NmFic (EC:2.7.7.n1)
Alternative name(s):
AMPylator NmFic
Gene namesi
Ordered Locus Names:NMB0255
OrganismiNeisseria meningitidis serogroup B (strain MC58)
Taxonomic identifieri122586 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
Proteomesi
  • UP000000425 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi182 – 1821S → A: Promotes adenylyltransferase activity; when associated with A-186. 1 Publication
Mutagenesisi186 – 1861E → A: Promotes adenylyltransferase activity; when associated with A-182. 2 Publications
Mutagenesisi186 – 1861E → G: Promotes adenylyltransferase activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191Adenosine monophosphate-protein transferase NmFicPRO_0000417551Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei183 – 1831O-AMP-tyrosine; in vitro1 Publication

Post-translational modificationi

Auto-AMPylation at Tyr-183 in vitro.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ7DDR9.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-60138N.
STRINGi122586.NMB0255.

Structurei

Secondary structure

1
191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2714Combined sources
Helixi30 – 334Combined sources
Beta strandi36 – 383Combined sources
Helixi39 – 5012Combined sources
Turni51 – 533Combined sources
Turni55 – 584Combined sources
Helixi75 – 8612Combined sources
Helixi93 – 10614Combined sources
Beta strandi109 – 1113Combined sources
Helixi113 – 12917Combined sources
Helixi135 – 1373Combined sources
Helixi140 – 14910Combined sources
Turni150 – 1523Combined sources
Helixi155 – 1628Combined sources
Beta strandi165 – 1673Combined sources
Helixi172 – 18514Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G03X-ray2.20A1-191[»]
3S6AX-ray2.20A11-191[»]
3SE5X-ray1.70A/B/C/D11-167[»]
3SN9X-ray3.03A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P11-191[»]
3ZLMX-ray2.00A11-191[»]
5CGLX-ray2.35A/B11-191[»]
5CKLX-ray0.99A11-191[»]
5CMTX-ray0.99A11-191[»]
ProteinModelPortaliQ7DDR9.
SMRiQ7DDR9. Positions 11-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7DDR9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 162126FidoPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi182 – 1876Inhibitory (S/T)XXXE(G/N) motif

Sequence similaritiesi

Contains 1 fido domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105MZU. Bacteria.
COG2184. LUCA.
HOGENOMiHOG000093879.
KOiK04095.
OMAiAKGNFRF.
OrthoDBiPOG091H04GI.

Family and domain databases

Gene3Di1.10.3290.10. 1 hit.
InterProiIPR003812. Fido.
[Graphical view]
PfamiPF02661. Fic. 1 hit.
[Graphical view]
SUPFAMiSSF140931. SSF140931. 1 hit.
PROSITEiPS51459. FIDO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7DDR9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSENPIGKT MKSIDEQSLH NARRLFESGD IDRIEVGTTA GLQQIHRYLF
60 70 80 90 100
GGLYDFAGQI REDNISKGGF RFANAMYLKE ALVKIEQMPE RTFEEIIAKY
110 120 130 140 150
VEMNIAHPFL EGNGRSTRIW LDLVLKKNLK KVVNWQNVSK TLYLQAMERS
160 170 180 190
PVNDLELRFL LKDNLTDDVD NREIIFKGIE QSYYYEGYEK G
Length:191
Mass (Da):22,190
Last modified:July 5, 2004 - v1
Checksum:iDAE3849D07424543
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF40709.1.
PIRiB81220.
RefSeqiNP_273311.1. NC_003112.2.
WP_002215631.1. NC_003112.2.

Genome annotation databases

EnsemblBacteriaiAAF40709; AAF40709; NMB0255.
GeneIDi902366.
KEGGinme:NMB0255.
PATRICi20355588. VBINeiMen85645_0318.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002098 Genomic DNA. Translation: AAF40709.1.
PIRiB81220.
RefSeqiNP_273311.1. NC_003112.2.
WP_002215631.1. NC_003112.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2G03X-ray2.20A1-191[»]
3S6AX-ray2.20A11-191[»]
3SE5X-ray1.70A/B/C/D11-167[»]
3SN9X-ray3.03A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P11-191[»]
3ZLMX-ray2.00A11-191[»]
5CGLX-ray2.35A/B11-191[»]
5CKLX-ray0.99A11-191[»]
5CMTX-ray0.99A11-191[»]
ProteinModelPortaliQ7DDR9.
SMRiQ7DDR9. Positions 11-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60138N.
STRINGi122586.NMB0255.

Proteomic databases

PaxDbiQ7DDR9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF40709; AAF40709; NMB0255.
GeneIDi902366.
KEGGinme:NMB0255.
PATRICi20355588. VBINeiMen85645_0318.

Phylogenomic databases

eggNOGiENOG4105MZU. Bacteria.
COG2184. LUCA.
HOGENOMiHOG000093879.
KOiK04095.
OMAiAKGNFRF.
OrthoDBiPOG091H04GI.

Enzyme and pathway databases

BioCyciNMEN122586:GHGG-270-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ7DDR9.

Family and domain databases

Gene3Di1.10.3290.10. 1 hit.
InterProiIPR003812. Fido.
[Graphical view]
PfamiPF02661. Fic. 1 hit.
[Graphical view]
SUPFAMiSSF140931. SSF140931. 1 hit.
PROSITEiPS51459. FIDO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNMFIC_NEIMB
AccessioniPrimary (citable) accession number: Q7DDR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: July 5, 2004
Last modified: September 7, 2016
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Defined as class III fido-domain containing proteins, in which the inhibitory helix is present at the C-terminus of the Fido domain.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.