BEPA_BARHE
ID BEPA_BARHE Reviewed; 544 AA.
AC Q6G2A9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein adenylyltransferase;
DE EC=2.7.7.n1 {ECO:0000269|PubMed:21213248};
DE AltName: Full=AMPylator;
GN Name=bepA; OrderedLocusNames=BH13370;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-302 IN COMPLEX WITH ATP,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21213248; DOI=10.1002/pro.581;
RA Palanivelu D.V., Goepfert A., Meury M., Guye P., Dehio C., Schirmer T.;
RT "Fic domain-catalyzed adenylylation: insight provided by the structural
RT analysis of the type IV secretion system effector BepA.";
RL Protein Sci. 20:492-499(2011).
CC -!- FUNCTION: Adenylyltransferase involved in virulence by mediating the
CC addition of adenosine 5'-monophosphate (AMP) to specific residue of
CC host target proteins. {ECO:0000269|PubMed:21213248}.
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:21213248};
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:21213248};
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Translocated into the host cell
CC via the type IV secretion system (T4SS).
CC -!- DOMAIN: The fido domain mediates the adenylyltransferase activity.
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DR EMBL; BX897699; CAF28110.1; -; Genomic_DNA.
DR RefSeq; WP_011181138.1; NZ_LRIJ02000001.1.
DR PDB; 2JK8; X-ray; 2.80 A; A/B=1-302.
DR PDB; 2VY3; X-ray; 2.80 A; A/B=1-302.
DR PDB; 2VZA; X-ray; 3.05 A; A/B/C/D/E/F/G/H=10-303.
DR PDB; 5NH2; X-ray; 2.32 A; A=10-303.
DR PDBsum; 2JK8; -.
DR PDBsum; 2VY3; -.
DR PDBsum; 2VZA; -.
DR PDBsum; 5NH2; -.
DR AlphaFoldDB; Q6G2A9; -.
DR SMR; Q6G2A9; -.
DR STRING; 283166.BH13370; -.
DR PaxDb; Q6G2A9; -.
DR PRIDE; Q6G2A9; -.
DR EnsemblBacteria; CAF28110; CAF28110; BH13370.
DR GeneID; 64157507; -.
DR KEGG; bhe:BH13370; -.
DR eggNOG; COG2184; Bacteria.
DR OMA; HYVYPNT; -.
DR EvolutionaryTrace; Q6G2A9; -.
DR Proteomes; UP000000421; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070733; F:protein adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0018117; P:protein adenylylation; IDA:UniProtKB.
DR Gene3D; 1.10.3290.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR040548; BepA_ID.
DR InterPro; IPR003812; Fido.
DR InterPro; IPR036597; Fido-like_dom_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR Pfam; PF02661; Fic; 1.
DR Pfam; PF18543; ID; 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 Secreted; Transferase; Virulence.
FT CHAIN 1..544
FT /note="Protein adenylyltransferase"
FT /id="PRO_0000417552"
FT DOMAIN 63..216
FT /note="Fido"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00791"
FT BINDING 93..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 106..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 163..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:21213248"
FT BINDING 170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:5NH2"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2JK8"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:5NH2"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5NH2"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 117..132
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:5NH2"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2JK8"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5NH2"
FT STRAND 253..261
FT /evidence="ECO:0007829|PDB:5NH2"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:5NH2"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5NH2"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:5NH2"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:5NH2"
SQ SEQUENCE 544 AA; 61341 MW; 81D675C74A1FC764 CRC64;
MPKAKAKTKN TEIISPHHYV YPNTTTLKNK YGIKNLNAFL EKCSHDTAKA MINLREESLP
EYFDTAYLCH IHQQLFKNTF EWAGYLRHIP FTFADGTTAA MPEMKRTGWK NAFAIGDEIQ
EGLQRLDQTL AEKNNLQGLT REEFNSEAIE LFNSLNQLHP FREGNGRTQR LFFENLAKAA
GHQLNFSLIT KERMMVASVA VAENGDLEPM QHLFEDISNP EKIRLLKEFM HTMKNTGRNV
NDRPVMVAKE GETYTGTYRG AGLEGFALNV KGAYIIGNID HLPPEQLKIL KPGDKITFTA
PKAEELKKTL IPKETLVPLT KLEIAEMVAE DAFVHTCRDQ ICSLSKIVYG SQGVLNKNII
EIIKNPSKGQ QLATQIERTP YSVHSLAGFD LICFKTGARV RAEKHVALLS CAVANFTHAV
KHARQEITKE HQAEQNRLRQ EVPMPSQSLQ DLLSLPKEFQ QKALGVSPLL QKELTSLLQK
VNSRLSSSEQ RALRENNHET LAKNLGVSEQ KAKEITKTVM KAREVQQKSQ TRTVSHSKTL
AMAS
