PEMI_ECOLX
ID PEMI_ECOLX Reviewed; 85 AA.
AC P13975;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Antitoxin PemI;
GN Name=pemI;
OS Escherichia coli.
OG Plasmid IncFII R100 (NR1), and Plasmid IncFII R1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=IncFII R100 (NR1);
RX PubMed=3019092; DOI=10.1016/0065-227x(86)90018-3;
RA Ohtsubo H., Ryder T.B., Maeda Y., Armstrong K., Ohtsubo E.;
RT "DNA replication of the resistance plasmid R100 and its control.";
RL Adv. Biophys. 21:115-133(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=IncFII R1;
RX PubMed=3323833; DOI=10.1007/bf00337764;
RA Bravo A., de Torrontegui G., Diaz R.;
RT "Identification of components of a new stability system of plasmid R1,
RT ParD, that is close to the origin of replication of this plasmid.";
RL Mol. Gen. Genet. 210:101-110(1987).
RN [3]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=2832364; DOI=10.1128/jb.170.4.1461-1466.1988;
RA Tsuchimoto S., Ohtsubo H., Ohtsubo E.;
RT "Two genes, pemK and pemI, responsible for stable maintenance of resistance
RT plasmid R100.";
RL J. Bacteriol. 170:1461-1466(1988).
RN [4]
RP CHARACTERIZATION.
RX PubMed=8455570; DOI=10.1007/bf00282787;
RA Tsuchimoto S., Ohtsubo E.;
RT "Autoregulation by cooperative binding of the PemI and PemK proteins to the
RT promoter region of the pem operon.";
RL Mol. Gen. Genet. 237:81-88(1993).
CC -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC Labile antitoxin that binds to its cognate PemK endoribonuclease toxin
CC and neutralizes its activity. Responsible for the stable maintenance of
CC the plasmid during cell division. Both PemI and PemK proteins bind to
CC the promoter region of the pem operon to autoregulate their synthesis.
CC {ECO:0000269|PubMed:2832364, ECO:0000269|PubMed:3323833,
CC ECO:0000269|PubMed:8455570}.
CC -!- SUBUNIT: Forms a complex with cognate toxin PemK.
CC {ECO:0000250|UniProtKB:P0AE72}.
CC -!- SIMILARITY: Belongs to the PemI family. {ECO:0000305}.
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DR EMBL; M26840; AAA26069.1; -; Genomic_DNA.
DR EMBL; X06240; CAA29584.1; -; Genomic_DNA.
DR PIR; I64783; I64783.
DR RefSeq; NP_862962.1; NC_004998.1.
DR RefSeq; NP_957646.1; NC_005327.1.
DR RefSeq; WP_000557619.1; NZ_WWEV01000284.1.
DR RefSeq; YP_001096514.1; NC_009133.1.
DR RefSeq; YP_001816576.1; NC_010558.1.
DR RefSeq; YP_002527568.1; NC_011964.1.
DR RefSeq; YP_003108264.1; NC_013121.1.
DR RefSeq; YP_003108328.1; NC_013122.1.
DR RefSeq; YP_003829175.1; NC_014384.1.
DR RefSeq; YP_003829285.1; NC_014385.1.
DR RefSeq; YP_003937672.1; NC_014615.1.
DR RefSeq; YP_006953466.1; NC_019073.1.
DR RefSeq; YP_006953884.1; NC_019089.1.
DR RefSeq; YP_006953889.1; NC_019090.1.
DR RefSeq; YP_006954226.1; NC_019095.1.
DR RefSeq; YP_007447504.1; NC_020278.2.
DR RefSeq; YP_008826479.1; NC_022885.1.
DR RefSeq; YP_009068666.1; NC_025141.1.
DR AlphaFoldDB; P13975; -.
DR BMRB; P13975; -.
DR SMR; P13975; -.
DR GeneID; 58464027; -.
DR OMA; NARERAW; -.
DR OrthoDB; 2047723at2; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR007159; SpoVT-AbrB_dom.
DR InterPro; IPR037914; SpoVT-AbrB_sf.
DR SMART; SM00966; SpoVT_AbrB; 1.
DR SUPFAM; SSF89447; SSF89447; 1.
DR PROSITE; PS51740; SPOVT_ABRB; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Plasmid; Toxin-antitoxin system.
FT CHAIN 1..85
FT /note="Antitoxin PemI"
FT /id="PRO_0000068412"
FT DOMAIN 4..49
FT /note="SpoVT-AbrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
SQ SEQUENCE 85 AA; 9333 MW; 8B216EAAFEAEE870 CRC64;
MHTTRLKRVG GSVMLTVPPA LLNALSLGTD NEVGMVIDNG RLIVEPYRRP QYSLAELLAQ
CDPNAEISAE EREWLDAPAT GQEEI