VBHT_BARSR
ID VBHT_BARSR Reviewed; 478 AA.
AC E6Z0R3;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Protein adenylyltransferase VbhT;
DE EC=2.7.7.n1 {ECO:0000269|PubMed:22266942, ECO:0000269|PubMed:23738009};
DE AltName: Full=AMPylator VbhT;
DE AltName: Full=Toxin VbhT {ECO:0000305};
GN Name=vbhT; ORFNames=B11C_100026;
OS Bartonella schoenbuchensis (strain DSM 13525 / NCTC 13165 / R1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=687861;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13525 / NCTC 13165 / R1;
RX PubMed=21347280; DOI=10.1371/journal.pgen.1001296;
RA Engel P., Salzburger W., Liesch M., Chang C.C., Maruyama S., Lanz C.,
RA Calteau A., Lajus A., Medigue C., Schuster S.C., Dehio C.;
RT "Parallel evolution of a type IV secretion system in radiating lineages of
RT the host-restricted bacterial pathogen Bartonella.";
RL PLoS Genet. 7:E1001296-E1001296(2011).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-198 IN COMPLEX WITH VBHA,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH VBHA, AND
RP MUTAGENESIS OF HIS-136.
RC STRAIN=DSM 13525 / NCTC 13165 / R1;
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 (1.94 ANGSTROMS) OF 1-198 IN COMPLEXES WITH MUTANT
RP VBHA ANTITOXIN; ATP AND MAGNESIUM, CATALYTIC ACTIVITY, AND SUBUNIT.
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: Toxic component of type II toxin-antitoxin (TA) system VbhT-
CC VbhA. Adenylyltransferase involved in virulence by mediating the
CC addition of adenosine 5'-monophosphate (AMP) to specific residue of
CC host GTPases. The resulting AMPylation affects GTPases, impairing actin
CC assembly in infected cells.
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
CC antitoxin VbhA; which acts by competing with ATP-binding at Arg-147 and
CC prevents productive ATP-binding. {ECO:0000269|PubMed:22266942}.
CC -!- SUBUNIT: Homodimer. Interacts with VbhA. {ECO:0000269|PubMed:22266942,
CC ECO:0000269|PubMed:23738009}.
CC -!- INTERACTION:
CC E6Z0R3; E6Z0R4: B11C_100027; NbExp=2; IntAct=EBI-15965345, EBI-15965363;
CC -!- DOMAIN: The fido domain mediates the adenylyltransferase activity.
CC -!- MISCELLANEOUS: Defined as class I fido-domain containing proteins, in
CC which the inhibitory helix is provided by an interacting antitoxin
CC (VbhA). {ECO:0000305|PubMed:22266942}.
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DR EMBL; FN645515; CBI82701.1; -; Genomic_DNA.
DR PDB; 3SHG; X-ray; 1.50 A; A=2-198.
DR PDB; 3ZC7; X-ray; 2.10 A; A=1-248.
DR PDB; 3ZCB; X-ray; 1.94 A; A=1-198.
DR PDBsum; 3SHG; -.
DR PDBsum; 3ZC7; -.
DR PDBsum; 3ZCB; -.
DR AlphaFoldDB; E6Z0R3; -.
DR SMR; E6Z0R3; -.
DR DIP; DIP-60136N; -.
DR IntAct; E6Z0R3; 1.
DR PRIDE; E6Z0R3; -.
DR BRENDA; 2.7.7.B23; 14828.
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; IPR041533; Bep_BID.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR Pfam; PF17841; Bep_C_terminal; 1.
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 Toxin-antitoxin system; Transferase; Virulence.
FT CHAIN 1..478
FT /note="Protein adenylyltransferase VbhT"
FT /id="PRO_0000417549"
FT DOMAIN 55..200
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT BINDING 85..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 133..136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 140..147
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 136
FT /note="H->A: Abolishes adenylyltransferase activity."
FT /evidence="ECO:0000269|PubMed:22266942"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:3SHG"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:3SHG"
FT HELIX 28..48
FT /evidence="ECO:0007829|PDB:3SHG"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:3SHG"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3SHG"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:3SHG"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:3SHG"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:3SHG"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:3SHG"
FT HELIX 118..135
FT /evidence="ECO:0007829|PDB:3SHG"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:3SHG"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:3SHG"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3SHG"
FT HELIX 168..179
FT /evidence="ECO:0007829|PDB:3SHG"
FT HELIX 184..192
FT /evidence="ECO:0007829|PDB:3SHG"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:3SHG"
SQ SEQUENCE 478 AA; 55379 MW; 01B426FDAFB7BC98 CRC64;
MRKYEGSNDP YTDPETGVMY NLLGIKDQAR LERVESAFAY IRSFELGRTS ISGKFDLDHM
KKIHKKLFGD VYEWAGKTRL VDIVKDNSKF AHYTQIESYA PQITQQLARE QHLRGLDANE
FSQRAGYYMG ELNALHPFRE GNGRTLREFI WQLAREAGYH IDWDRVERQE MTRASIESYY
GNSDLMSALI RRNLTEFTVN RRVDVSQGIN ERVLSHIDID KEWPQKGFNI AIQTTQQAPY
LSSYTDTSNL EEKAQNALRN EQSYVDTFKE LNDHLKTIYK DPQAAALKIE QTILAGKGDK
LPDILAKAPN KVGELRGSDR LIDKLKSAGK ERKAALYNVP LAISTIRRLQ SFYKNSYEKH
MDKLTREREQ LKVEVPSLSQ EAVAYMKNVE VGRNNYSKIP ENINKEFVQL ESALNRRFGK
DVIYKRNFNL SKEIASKQTY DKKLVNELQT AIKFLQQRHI QKQNNLAITR TPSKGITR
