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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)DescriptionActionsGraphical viewLength
Binding sitei67ATP1 Publication1
Binding sitei186ATP1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi104 – 107ATP1 Publication4
Nucleotide bindingi112 – 118ATP1 Publication7
Nucleotide bindingi140 – 143ATP1 Publication4

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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)DescriptionActionsGraphical viewLength
Mutagenesisi182S → A: Promotes adenylyltransferase activity; when associated with A-186. 1 Publication1
Mutagenesisi186E → A: Promotes adenylyltransferase activity; when associated with A-182. 2 Publications1
Mutagenesisi186E → G: Promotes adenylyltransferase activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004175511 – 191Adenosine monophosphate-protein transferase NmFicAdd BLAST191

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei183O-AMP-tyrosine; in vitro1 Publication1

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

1191
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi14 – 27Combined sources14
Helixi30 – 33Combined sources4
Beta strandi36 – 38Combined sources3
Helixi39 – 50Combined sources12
Turni51 – 53Combined sources3
Turni55 – 58Combined sources4
Helixi75 – 86Combined sources12
Helixi93 – 106Combined sources14
Beta strandi109 – 111Combined sources3
Helixi113 – 129Combined sources17
Helixi135 – 137Combined sources3
Helixi140 – 149Combined sources10
Turni150 – 152Combined sources3
Helixi155 – 162Combined sources8
Beta strandi165 – 167Combined sources3
Helixi172 – 185Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7DDR9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini37 – 162FidoPROSITE-ProRule annotationAdd BLAST126

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi182 – 187Inhibitory (S/T)XXXE(G/N) motif6

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
PDB 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.
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.

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: November 30, 2016
This is version 78 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.