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Protein

Adenosine monophosphate-protein transferase VbhT

Gene

vbhT

Organism
Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Toxic component of a toxin-antitoxin (TA) module VbhT-VbhA. Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific residue of host GTPases. The resulting AMPylation affects GTPases, impairing actin assembly in infected cells.

Catalytic activityi

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

Enzyme regulationi

Adenylyltransferase activity is inhibited by antitoxin VbhA; which acts by competing with ATP-binding at Arg-147 and prevents productive ATP-binding.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei175ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi85 – 88ATP4
Nucleotide bindingi133 – 136ATP4
Nucleotide bindingi140 – 147ATP8

GO - Molecular functioni

GO - Biological processi

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

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Virulence

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine monophosphate-protein transferase VbhT (EC:2.7.7.n1)
Alternative name(s):
AMPylator VbhT
Gene namesi
Name:vbhT
ORF Names:B11C_100026
OrganismiBartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1)
Taxonomic identifieri687861 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi136H → A: Abolishes adenylyltransferase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004175491 – 478Adenosine monophosphate-protein transferase VbhTAdd BLAST478

Interactioni

Subunit structurei

Homodimer. Interacts with VbhA.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-60136N.

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Turni14 – 16Combined sources3
Helixi28 – 48Combined sources21
Helixi57 – 68Combined sources12
Turni69 – 71Combined sources3
Turni73 – 76Combined sources4
Helixi93 – 95Combined sources3
Helixi96 – 109Combined sources14
Helixi111 – 113Combined sources3
Helixi118 – 135Combined sources18
Beta strandi138 – 140Combined sources3
Helixi142 – 156Combined sources15
Beta strandi159 – 161Combined sources3
Helixi168 – 179Combined sources12
Helixi184 – 192Combined sources9
Beta strandi194 – 196Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SHGX-ray1.50A2-198[»]
3ZC7X-ray2.10A1-248[»]
3ZCBX-ray1.94A1-198[»]
SMRiE6Z0R3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 200FidoPROSITE-ProRule annotationAdd BLAST146

Domaini

The fido domain mediates the adenylyltransferase activity.

Sequence similaritiesi

Contains 1 fido domain.PROSITE-ProRule annotation

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.

E6Z0R3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKYEGSNDP YTDPETGVMY NLLGIKDQAR LERVESAFAY IRSFELGRTS
60 70 80 90 100
ISGKFDLDHM KKIHKKLFGD VYEWAGKTRL VDIVKDNSKF AHYTQIESYA
110 120 130 140 150
PQITQQLARE QHLRGLDANE FSQRAGYYMG ELNALHPFRE GNGRTLREFI
160 170 180 190 200
WQLAREAGYH IDWDRVERQE MTRASIESYY GNSDLMSALI RRNLTEFTVN
210 220 230 240 250
RRVDVSQGIN ERVLSHIDID KEWPQKGFNI AIQTTQQAPY LSSYTDTSNL
260 270 280 290 300
EEKAQNALRN EQSYVDTFKE LNDHLKTIYK DPQAAALKIE QTILAGKGDK
310 320 330 340 350
LPDILAKAPN KVGELRGSDR LIDKLKSAGK ERKAALYNVP LAISTIRRLQ
360 370 380 390 400
SFYKNSYEKH MDKLTREREQ LKVEVPSLSQ EAVAYMKNVE VGRNNYSKIP
410 420 430 440 450
ENINKEFVQL ESALNRRFGK DVIYKRNFNL SKEIASKQTY DKKLVNELQT
460 470
AIKFLQQRHI QKQNNLAITR TPSKGITR
Length:478
Mass (Da):55,379
Last modified:March 8, 2011 - v1
Checksum:i01B426FDAFB7BC98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN645515 Genomic DNA. Translation: CBI82701.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FN645515 Genomic DNA. Translation: CBI82701.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SHGX-ray1.50A2-198[»]
3ZC7X-ray2.10A1-248[»]
3ZCBX-ray1.94A1-198[»]
SMRiE6Z0R3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60136N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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 nameiVBHT_BARSR
AccessioniPrimary (citable) accession number: E6Z0R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2012
Last sequence update: March 8, 2011
Last modified: November 30, 2016
This is version 18 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 I fido-domain containing proteins, in which the inhibitory helix is provided by an interacting antitoxin (VbhA).1 Publication

Keywords - Technical termi

3D-structure

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.