PART_SPHYB
ID PART_SPHYB Reviewed; 161 AA.
AC A0A0C5XL88;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Prs ADP-ribosylating toxin {ECO:0000303|PubMed:30598453};
DE EC=2.4.2.- {ECO:0000269|PubMed:30598453};
DE AltName: Full=Mono-ADP-ribosyltransferase {ECO:0000303|PubMed:30598453};
DE Short=mART {ECO:0000303|PubMed:30598453};
GN Name=parT {ECO:0000303|PubMed:30598453};
GN Synonyms=yblI {ECO:0000303|PubMed:30598453}; ORFNames=TZ53_17660;
OS Sphingobium sp. (strain YBL2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=484429;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YBL2;
RA Yan X.;
RT "The analysis of one genome.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:6D0H, ECO:0007744|PDB:6D0I}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-159 IN COMPLEX WITH ANTITOXIN
RP FRAGMENT, FUNCTION AS A TOXIN, CATALYTIC ACTIVITY, EXPRESSION IN E.COLI,
RP DOMAIN, AUTO-ADP-RIBOSYLATION, AND MUTAGENESIS OF SER-21; ARG-31; TYR-41;
RP SER-44; SER-45; GLU-52; HIS-56; SER-122; 127-GLU-GLU-128; GLU-127 AND
RP GLU-128.
RC STRAIN=YBL2;
RX PubMed=30598453; DOI=10.1073/pnas.1814633116;
RA Piscotta F.J., Jeffrey P.D., Link A.J.;
RT "ParST is a widespread toxin-antitoxin module that targets nucleotide
RT metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:826-834(2019).
CC -!- FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system.
CC Expression in E.coli inhibits cell growth; bacteriostasis is
CC neutralized by expression of cognate antitoxin ParS. ADP-ribosylates
CC E.coli ribose-phosphate pyrophosphokinase (RPPK, prs) using NAD(+) in
CC vitro; ADP-ribosylates RPPK on 'Lys-182' and 'Ser-202'. Cannot use
CC NADP(+). Also auto-ADP-ribosylates in vitro; in the presence of RPPK
CC auto-ADP-ribosylation decreases. {ECO:0000269|PubMed:30598453}.
CC -!- SUBUNIT: Homodimer, forms heterotetrameric ParS(2)-ParT(2) complexes.
CC {ECO:0000269|PubMed:30598453}.
CC -!- DOMAIN: Forms salt bridges between the 2 toxin molecules mediated by
CC Glu-127 Glu-128 on one subunit and Arg-46 Arg-149 on the other.
CC {ECO:0000269|PubMed:30598453}.
CC -!- PTM: Consumes NAD(+) and auto-ADP-ribosylates on the tryptic fragment
CC Ala-47-Arg-66 in vitro. Also auto-ADP-ribosylates using NADP(+).
CC {ECO:0000269|PubMed:30598453}.
CC -!- SIMILARITY: Belongs to the MbcT/ParT/Res family. {ECO:0000305}.
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DR EMBL; CP010954; AJR25280.1; -; Genomic_DNA.
DR RefSeq; WP_044662136.1; NZ_CP010954.1.
DR PDB; 6D0H; X-ray; 1.50 A; A/C=2-159.
DR PDB; 6D0I; X-ray; 1.55 A; A/C=2-159.
DR PDBsum; 6D0H; -.
DR PDBsum; 6D0I; -.
DR AlphaFoldDB; A0A0C5XL88; -.
DR SMR; A0A0C5XL88; -.
DR STRING; 484429.TZ53_17660; -.
DR EnsemblBacteria; AJR25280; AJR25280; TZ53_17660.
DR KEGG; syb:TZ53_17660; -.
DR PATRIC; fig|484429.4.peg.3699; -.
DR HOGENOM; CLU_133611_0_0_5; -.
DR OrthoDB; 1821714at2; -.
DR Proteomes; UP000032302; Chromosome.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR014914; RES_dom.
DR Pfam; PF08808; RES; 1.
DR SMART; SM00953; RES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Toxin-antitoxin system; Transferase.
FT CHAIN 1..161
FT /note="Prs ADP-ribosylating toxin"
FT /id="PRO_0000448605"
FT MUTAGEN 21
FT /note="S->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 31
FT /note="R->A: No longer toxic, greatly decreased auto-ADP-
FT ribosylation."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 41
FT /note="Y->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 44
FT /note="S->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 45
FT /note="S->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 52
FT /note="E->A: No longer toxic."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 56
FT /note="H->A: No longer toxic."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 122
FT /note="S->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 127..128
FT /note="EE->AA: No longer toxic."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 127
FT /note="E->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:30598453"
FT MUTAGEN 128
FT /note="E->A: No change in toxicity."
FT /evidence="ECO:0000269|PubMed:30598453"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:6D0H"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:6D0H"
FT HELIX 23..28
FT /evidence="ECO:0007829|PDB:6D0H"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:6D0H"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:6D0H"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:6D0H"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:6D0H"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:6D0H"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6D0H"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:6D0H"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:6D0H"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:6D0H"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6D0H"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:6D0H"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:6D0H"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:6D0H"
SQ SEQUENCE 161 AA; 17408 MW; B926D2237639A142 CRC64;
MTTSFWRIAT DARTYEADDL SGAGAKITGG RWNEVGVAIV YAASSRALAC LETVVHLNSG
GLPLNRYLVE IEVPDEVLAS AEVATPGNLP VGWDAEPAGR VSISFGSQWA QSQRTALLLV
PSVIVPEETN LLINPAHPDA KGIKARKVRK WLYDPRMIRK A
