ID   PRLF_ECOLI              Reviewed;         111 AA.
AC   P15373; Q2M980;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Antitoxin PrlF;
DE   AltName: Full=HtrA suppressor protein SohA;
GN   Name=prlF; Synonyms=sohA; OrderedLocusNames=b3129, JW3098;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUPPRESSION OF JAMMED SECRETION
RP   MACHINERY, MUTAGENESIS OF 91-GLN--GLU-111, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=2152898; DOI=10.1128/jb.172.1.185-192.1990;
RA   Kiino D.R., Phillips G.J., Silhavy T.J.;
RT   "Increased expression of the bifunctional protein PrlF suppresses
RT   overproduction lethality associated with exported beta-galactosidase hybrid
RT   proteins in Escherichia coli.";
RL   J. Bacteriol. 172:185-192(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND SUPPRESSION OF AN
RP   HTRA NULL MUTANT.
RC   STRAIN=K12;
RX   PubMed=2407727; DOI=10.1128/jb.172.3.1587-1594.1990;
RA   Baird L., Georgopoulos C.;
RT   "Identification, cloning, and characterization of the Escherichia coli sohA
RT   gene, a suppressor of the htrA (degP) null phenotype.";
RL   J. Bacteriol. 172:1587-1594(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION AS AN ANTITOXIN, SUBUNIT, DNA-BINDING, AND OPERON STRUCTURE.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=17706670; DOI=10.1016/j.jmb.2007.07.016;
RA   Schmidt O., Schuenemann V.J., Hand N.J., Silhavy T.J., Martin J.,
RA   Lupas A.N., Djuranovic S.;
RT   "prlF and yhaV encode a new toxin-antitoxin system in Escherichia coli.";
RL   J. Mol. Biol. 372:894-905(2007).
RN   [6]
RP   REVIEW.
RX   PubMed=19215780; DOI=10.1016/s0079-6603(08)00812-x;
RA   Yamaguchi Y., Inouye M.;
RT   "mRNA interferases, sequence-specific endoribonucleases from the toxin-
RT   antitoxin systems.";
RL   Prog. Mol. Biol. Transl. Sci. 85:467-500(2009).
CC   -!- FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system.
CC       Labile antitoxin that binds to the YhaV toxin and neutralizes its
CC       ribonuclease activity. Also acts as a transcription factor. The
CC       YhaV/PrlF complex binds the prlF-yhaV operon, probably negatively
CC       regulating its expression. {ECO:0000269|PubMed:17706670}.
CC   -!- FUNCTION: Negatively regulates its own expression as well as relieving
CC       the export block imposed by high-level synthesis of the LamB-LacZ
CC       hybrid protein. Overexpression leads to increased doubling time and
CC       also suppresses a htrA (degP) null phenotype.
CC       {ECO:0000269|PubMed:17706670}.
CC   -!- SUBUNIT: Homodimer; forms a complex with YhaV with stoichiometry
CC       PrlF(2)-YhaV(4), possibly as a YhaV(2)-PrlF(2)-YhaV(2) complex like the
CC       MazFE complex. This complex is seen to dimerize in solution.
CC       {ECO:0000269|PubMed:17706670}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Not essential. {ECO:0000269|PubMed:2152898}.
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DR   EMBL; M30178; AAA24638.1; -; Genomic_DNA.
DR   EMBL; M32358; AAA24418.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA57932.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76163.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77176.1; -; Genomic_DNA.
DR   PIR; A35137; A35137.
DR   RefSeq; NP_417598.1; NC_000913.3.
DR   RefSeq; WP_001307405.1; NZ_STEB01000001.1.
DR   AlphaFoldDB; P15373; -.
DR   SMR; P15373; -.
DR   BioGRID; 4259492; 399.
DR   BioGRID; 851952; 3.
DR   ComplexPortal; CPX-4102; PrlF-YhaV toxin-antitoxin complex.
DR   IntAct; P15373; 6.
DR   STRING; 511145.b3129; -.
DR   jPOST; P15373; -.
DR   PaxDb; P15373; -.
DR   PRIDE; P15373; -.
DR   DNASU; 947639; -.
DR   EnsemblBacteria; AAC76163; AAC76163; b3129.
DR   EnsemblBacteria; BAE77176; BAE77176; BAE77176.
DR   GeneID; 66672972; -.
DR   GeneID; 947639; -.
DR   KEGG; ecj:JW3098; -.
DR   KEGG; eco:b3129; -.
DR   PATRIC; fig|1411691.4.peg.3602; -.
DR   EchoBASE; EB0948; -.
DR   eggNOG; COG2002; Bacteria.
DR   HOGENOM; CLU_143957_0_0_6; -.
DR   InParanoid; P15373; -.
DR   OMA; DKICYTI; -.
DR   PhylomeDB; P15373; -.
DR   BioCyc; EcoCyc:EG10955-MON; -.
DR   BioCyc; MetaCyc:EG10955-MON; -.
DR   PRO; PR:P15373; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0110001; C:toxin-antitoxin complex; IPI:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR   GO; GO:0019899; F:enzyme binding; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0097351; F:toxin sequestering activity; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR   GO; GO:0001558; P:regulation of cell growth; IMP:EcoCyc.
DR   GO; GO:0040008; P:regulation of growth; IC:ComplexPortal.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR   GO; GO:0044010; P:single-species biofilm formation; IDA:ComplexPortal.
DR   InterPro; IPR031848; PrlF_antitoxin.
DR   InterPro; IPR007159; SpoVT-AbrB_dom.
DR   InterPro; IPR037914; SpoVT-AbrB_sf.
DR   Pfam; PF15937; PrlF_antitoxin; 1.
DR   SUPFAM; SSF89447; SSF89447; 1.
DR   PROSITE; PS51740; SPOVT_ABRB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Reference proteome; Repressor;
KW   Toxin-antitoxin system; Transcription; Transcription regulation.
FT   CHAIN           1..111
FT                   /note="Antitoxin PrlF"
FT                   /id="PRO_0000072033"
FT   DOMAIN          12..59
FT                   /note="SpoVT-AbrB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01076"
FT   MUTAGEN         91..111
FT                   /note="QGKKLVAGMDVNIDDEIGDDE->HSTRKETCRWHGRQH: In prlF1;
FT                   suppresses overproduction lethality of lamB-lacZ gene
FT                   fusions, leads to decreased beta-galactosidase activity.
FT                   Partially alleviates YhaV toxic activity."
FT                   /evidence="ECO:0000269|PubMed:2152898"
SQ   SEQUENCE   111 AA;  12359 MW;  5FC0D5FF43F75D8A CRC64;
     MPANARSHAV LTTESKVTIR GQTTIPAPVR EALKLKPGQD SIHYEILPGG QVFMCRLGDE
     QEDHTMNAFL RFLDADIQNN PQKTRPFNIQ QGKKLVAGMD VNIDDEIGDD E