ARGP_ECOLI
ID ARGP_ECOLI Reviewed; 297 AA.
AC P0A8S1; P24194; Q2M9S6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=HTH-type transcriptional regulator ArgP {ECO:0000255|HAMAP-Rule:MF_00513, ECO:0000305};
DE AltName: Full=Inhibitor of chromosome initiation {ECO:0000303|PubMed:2034653};
DE AltName: Full=OriC replication inhibitor;
GN Name=argP {ECO:0000255|HAMAP-Rule:MF_00513, ECO:0000303|PubMed:10600368};
GN Synonyms=iciA {ECO:0000303|PubMed:2034653};
GN OrderedLocusNames=b2916, JW2883;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-41.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2034653; DOI=10.1073/pnas.88.10.4066;
RA Thoeny B., Hwang D.S., Fradkin L., Kornberg A.;
RT "iciA, an Escherichia coli gene encoding a specific inhibitor of
RT chromosomal initiation of replication in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4066-4070(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Roy I., Leadlay P.F.;
RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-176.
RC STRAIN=K12;
RX PubMed=8366047; DOI=10.1128/jb.175.17.5628-5635.1993;
RA Hove-Jensen B., Maigaard M.;
RT "Escherichia coli rpiA gene encoding ribose phosphate isomerase A.";
RL J. Bacteriol. 175:5628-5635(1993).
RN [6]
RP BINDING TO ORIC, SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=1733927; DOI=10.1016/s0021-9258(18)45863-2;
RA Hwang D.S., Thoeny B., Kornberg A.;
RT "IciA protein, a specific inhibitor of initiation of Escherichia coli
RT chromosomal replication.";
RL J. Biol. Chem. 267:2209-2213(1992).
RN [7]
RP CLEAVAGE BY DEGP.
RX PubMed=8335089; DOI=10.1016/0014-5793(93)81029-y;
RA Yoo S.J., Seol J.H., Woo S.K., Suh S.W., Hwang D.S., Ha D.B., Chung C.H.;
RT "Hydrolysis of the IciA protein, an inhibitor of DNA replication
RT initiation, by protease Do in Escherichia coli.";
RL FEBS Lett. 327:17-20(1993).
RN [8]
RP PUTATIVE FUNCTION IN REGULATION OF DNAA EXPRESSION, AND DNA-BINDING.
RX PubMed=9254708; DOI=10.1093/nar/25.17.3486;
RA Lee Y., Lee H., Yim J., Hwang D.;
RT "The binding of two dimers of IciA protein to the dnaA promoter 1P element
RT enhances the binding of RNA polymerase to the dnaA promoter 1P.";
RL Nucleic Acids Res. 25:3486-3489(1997).
RN [9]
RP PUTATIVE FUNCTION IN REGULATION OF NRD EXPRESSION, AND DNA-BINDING.
RX PubMed=9819053; DOI=10.1007/s004380050854;
RA Han J.S., Kwon H.S., Yim J.B., Hwang D.S.;
RT "Effect of IciA protein on the expression of the nrd gene encoding
RT ribonucleoside diphosphate reductase in E. coli.";
RL Mol. Gen. Genet. 259:610-614(1998).
RN [10]
RP DNA-BINDING.
RX PubMed=10551881; DOI=10.1074/jbc.274.46.33105;
RA Azam T.A., Ishihama A.;
RT "Twelve species of the nucleoid-associated protein from Escherichia coli.
RT Sequence recognition specificity and DNA binding affinity.";
RL J. Biol. Chem. 274:33105-33113(1999).
RN [11]
RP FUNCTION IN REGULATION OF ARGK EXPRESSION, AND DNA-BINDING.
RX PubMed=10600368; DOI=10.1006/jmbi.1999.3308;
RA Celis R.T.;
RT "Repression and activation of arginine transport genes in Escherichia coli
RT K 12 by the ArgP protein.";
RL J. Mol. Biol. 294:1087-1095(1999).
RN [12]
RP FUNCTION IN REGULATION OF ARGO EXPRESSION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15150242; DOI=10.1128/jb.186.11.3539-3546.2004;
RA Nandineni M.R., Gowrishankar J.;
RT "Evidence for an arginine exporter encoded by yggA (argO) that is regulated
RT by the LysR-type transcriptional regulator ArgP in Escherichia coli.";
RL J. Bacteriol. 186:3539-3546(2004).
RN [13]
RP FUNCTION IN REGULATION OF ARGO EXPRESSION, AND DNA-BINDING.
RX PubMed=17504942; DOI=10.1101/gad.1520507;
RA Laishram R.S., Gowrishankar J.;
RT "Environmental regulation operating at the promoter clearance step of
RT bacterial transcription.";
RL Genes Dev. 21:1258-1272(2007).
RN [14]
RP FUNCTION IN REGULATION OF LYSP EXPRESSION, AND DNA-BINDING.
RC STRAIN=K12;
RX PubMed=21441513; DOI=10.1128/jb.00815-10;
RA Ruiz J., Haneburger I., Jung K.;
RT "Identification of ArgP and Lrp as transcriptional regulators of lysP, the
RT gene encoding the specific lysine permease of Escherichia coli.";
RL J. Bacteriol. 193:2536-2548(2011).
RN [15]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=21890697; DOI=10.1128/jb.05869-11;
RA Marbaniang C.N., Gowrishankar J.;
RT "Role of ArgP (IciA) in lysine-mediated repression in Escherichia coli.";
RL J. Bacteriol. 193:5985-5996(2011).
CC -!- FUNCTION: Controls the transcription of genes involved in arginine and
CC lysine metabolism. Activates transcription of several genes, including
CC argO, lysP, lysC, asd, dapB, dapD, lysA, gdhA and argK. Acts by binding
CC directly to their promoter or control region (PubMed:10600368,
CC PubMed:15150242, PubMed:17504942, PubMed:21441513, PubMed:21890697).
CC ArgP dimer by itself is able to bind the argO promoter-operator region
CC to form a binary complex, but the formation of a ternary complex with
CC RNA polymerase is greatly stimulated only in presence of a coeffector.
CC Both arginine and lysine are coeffectors at the argO promoter, but only
CC arginine is competent to activate transcription. Lysine has repressive
CC effects (PubMed:15150242, PubMed:17504942). ArgP also mediates lysine
CC repression of dapB, and gdhA in vivo, but via an alternative mechanism:
CC ArgP binding is directly reduced upon the addition of lysine
CC (PubMed:21890697). Binds in vitro to the promoter region of dnaA and to
CC the upstream region of the nrd promoter, but these genes are probably
CC not regulated by ArgP in vivo (PubMed:9254708, PubMed:9819053,
CC PubMed:21890697). In vitro, binds also to the three 13-mers located in
CC the origin region (oriC) and blocks the initiation of replication
CC (PubMed:1733927). {ECO:0000269|PubMed:10600368,
CC ECO:0000269|PubMed:15150242, ECO:0000269|PubMed:1733927,
CC ECO:0000269|PubMed:17504942, ECO:0000269|PubMed:21441513,
CC ECO:0000269|PubMed:21890697, ECO:0000269|PubMed:9254708,
CC ECO:0000269|PubMed:9819053}.
CC -!- ACTIVITY REGULATION: Specifically cleaved by the protease DegP. Cleaved
CC ArgP can no longer interact with the oriC region in vitro. Cleavage may
CC play an important role in the control of the protein availability.
CC {ECO:0000269|PubMed:8335089}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00513,
CC ECO:0000269|PubMed:1733927}.
CC -!- DEVELOPMENTAL STAGE: The amount of protein increases in the late
CC logarithmic phase. {ECO:0000269|PubMed:1733927}.
CC -!- DISRUPTION PHENOTYPE: Null mutants are more sensitive to canavanine.
CC {ECO:0000269|PubMed:15150242}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; M62865; AAA62780.1; -; Genomic_DNA.
DR EMBL; X66836; CAA47310.1; -; Genomic_DNA.
DR EMBL; U28377; AAA69083.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75953.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76980.1; -; Genomic_DNA.
DR EMBL; X73026; CAA51508.1; -; Genomic_DNA.
DR PIR; S22098; S22098.
DR RefSeq; NP_417391.1; NC_000913.3.
DR RefSeq; WP_000828351.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0A8S1; -.
DR SMR; P0A8S1; -.
DR BioGRID; 4263054; 80.
DR DIP; DIP-48015N; -.
DR IntAct; P0A8S1; 8.
DR STRING; 511145.b2916; -.
DR jPOST; P0A8S1; -.
DR PaxDb; P0A8S1; -.
DR PRIDE; P0A8S1; -.
DR EnsemblBacteria; AAC75953; AAC75953; b2916.
DR EnsemblBacteria; BAE76980; BAE76980; BAE76980.
DR GeneID; 66673207; -.
DR GeneID; 944867; -.
DR KEGG; ecj:JW2883; -.
DR KEGG; eco:b2916; -.
DR PATRIC; fig|1411691.4.peg.3816; -.
DR EchoBASE; EB0485; -.
DR eggNOG; COG0583; Bacteria.
DR HOGENOM; CLU_063829_0_0_6; -.
DR InParanoid; P0A8S1; -.
DR OMA; QQWKLDS; -.
DR PhylomeDB; P0A8S1; -.
DR BioCyc; EcoCyc:EG10490-MON; -.
DR PRO; PR:P0A8S1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003681; F:bent DNA binding; IDA:EcoliWiki.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoliWiki.
DR GO; GO:0032297; P:negative regulation of DNA-templated DNA replication initiation; IDA:EcoCyc.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00513; HTH_type_ArgP; 1.
DR InterPro; IPR017685; ArgP.
DR InterPro; IPR023490; ArgP_Gammaproteobact.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR TIGRFAMs; TIGR03298; argP; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 1: Evidence at protein level;
KW Activator; Direct protein sequencing; DNA-binding; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..297
FT /note="HTH-type transcriptional regulator ArgP"
FT /id="PRO_0000105641"
FT DOMAIN 4..60
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00513"
FT DNA_BIND 21..40
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00513"
SQ SEQUENCE 297 AA; 33472 MW; 8AD60B7B6661E3EF CRC64;
MKRPDYRTLQ ALDAVIRERG FERAAQKLCI TQSAVSQRIK QLENMFGQPL LVRTVPPRPT
EQGQKLLALL RQVELLEEEW LGDEQTGSTP LLLSLAVNAD SLATWLLPAL APVLADSPIR
LNLQVEDETR TQERLRRGEV VGAVSIQHQA LPSCLVDKLG ALDYLFVSSK PFAEKYFPNG
VTRSALLKAP VVAFDHLDDM HQAFLQQNFD LPPGSVPCHI VNSSEAFVQL ARQGTTCCMI
PHLQIEKELA SGELIDLTPG LFQRRMLYWH RFAPESRMMR KVTDALLDYG HKVLRQD
