ID   SERDT_BPSAV             Reviewed;         411 AA.
AC   E1XTK6;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Serinyltransferase {ECO:0000305};
DE   AltName: Full=Amino acid:DNA transferase {ECO:0000303|PubMed:34522950};
DE            Short=AADT {ECO:0000303|PubMed:34522950};
DE   AltName: Full=gp247 {ECO:0000303|PubMed:34522950};
GN   ORFNames=Vi01_199 {ECO:0000312|EMBL:CBW38065.1};
OS   Salmonella phage ViI.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Ackermannviridae; Cvivirinae; Kuttervirus.
OX   NCBI_TaxID=1987993;
OH   NCBI_TaxID=90370; Salmonella typhi.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20817773; DOI=10.1128/jb.00659-10;
RA   Pickard D., Toribio A.L., Petty N.K., van Tonder A., Yu L., Goulding D.,
RA   Barrell B., Rance R., Harris D., Wetter M., Wain J., Choudhary J.,
RA   Thomson N., Dougan G.;
RT   "A conserved acetyl esterase domain targets diverse bacteriophages to the
RT   Vi capsular receptor of Salmonella enterica serovar Typhi.";
RL   J. Bacteriol. 192:5746-5754(2010).
RN   [2]
RP   FUNCTION.
RX   PubMed=29555775; DOI=10.1073/pnas.1714812115;
RA   Lee Y.J., Dai N., Walsh S.E., Mueller S., Fraser M.E., Kauffman K.M.,
RA   Guan C., Correa I.R. Jr., Weigele P.R.;
RT   "Identification and biosynthesis of thymidine hypermodifications in the
RT   genomic DNA of widespread bacterial viruses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E3116-E3125(2018).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-282 AND CYS-287.
RX   PubMed=34522950; DOI=10.1093/nar/gkab781;
RA   Lee Y.J., Dai N., Mueller S.I., Guan C., Parker M.J., Fraser M.E.,
RA   Walsh S.E., Sridar J., Mulholland A., Nayak K., Sun Z., Lin Y.C.,
RA   Comb D.G., Marks K., Gonzalez R., Dowling D.P., Bandarian V., Saleh L.,
RA   Correa I.R., Weigele P.R.;
RT   "Pathways of thymidine hypermodification.";
RL   Nucleic Acids Res. 0:0-0(2021).
CC   -!- FUNCTION: Transfers serine to 5-phosphomethyl-2'-deoxyuridine (5-PmdU)
CC       to produce 5-O-serinylthymidine (O-SerT) as a step in the pathway
CC       leading to thymidine hypermodifications in the viral genome
CC       (PubMed:34522950). As a final result of the pathway of
CC       hypermodification, 5-aminoethoxy-2'-deoxymethyluridine (5-NeOmdU)
CC       substitutes for about 40% of the thymidines in the viral DNA
CC       (PubMed:34522950, PubMed:29555775). These modifications probably
CC       prevent degradation of viral genome by the host restriction-
CC       modification antiviral defense system (PubMed:34522950).
CC       {ECO:0000269|PubMed:29555775, ECO:0000269|PubMed:34522950}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phosphomethyl-dUMP in DNA + L-serine = 5-O-(L-seryl)-dTMP in
CC         DNA + phosphate; Xref=Rhea:RHEA:71567, Rhea:RHEA-COMP:18039,
CC         Rhea:RHEA-COMP:18046, ChEBI:CHEBI:33384, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:190918, ChEBI:CHEBI:190922;
CC         Evidence={ECO:0000269|PubMed:34522950};
CC   -!- SIMILARITY: Belongs to the thymidine aminotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; FQ312032; CBW38065.1; -; Genomic_DNA.
DR   Proteomes; UP000000339; Genome.
DR   InterPro; IPR040741; Alpha_GPT-Pplase2.
DR   Pfam; PF18724; aGPT-Pplase2; 1.
PE   1: Evidence at protein level;
KW   Host-virus interaction; Reference proteome;
KW   Restriction-modification system evasion by virus; Transferase.
FT   CHAIN           1..411
FT                   /note="Serinyltransferase"
FT                   /id="PRO_0000456274"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000305|PubMed:34522950"
FT   MUTAGEN         282
FT                   /note="E->A: Complete loss of enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:34522950"
FT   MUTAGEN         287
FT                   /note="C->A: Complete loss of enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:34522950"
SQ   SEQUENCE   411 AA;  48718 MW;  CA03A6A41A1E8561 CRC64;
     MTHLSKMPTG YTPPAEWKYP IDLSIDYRKP ENRMYLLKAW VEALSYTEEH NQQVRLMDYA
     IEVTEGITQL EKIERKIWMA FLWGCCYNGI GPWTIYSEFP VPPQSPQEFK RFCDWYNLNF
     ERMRFDTDCR YRKSKMIPCV QSYIDWLAGR TQMDAFRPLL ETKLQSDQFV KLWDTAMGWK
     YFGRLSAWNF LEALNMVFGN MYQIDVPGFM LRDRDGSESN RNGAAFLSNR DDWVTKHGKK
     KINGCPITDE ECDILEADLE QAFKDCVAEF GHITFINRLN FETSGACWLK KFFRLKNTRY
     IGWDAERTWD EIDYMERIWP EYSCKALWEA RSLWLPDTLL CEKAPAGHVP GVQKWKMPVF
     FETGVPLHIW HLQQGTRWEP SEVYTNLKMP VRKIDDNPKS TSVNLMSLLK R