SXY_ECOLI
ID SXY_ECOLI Reviewed; 209 AA.
AC P75869;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein Sxy;
DE AltName: Full=Competence activator Sxy {ECO:0000303|PubMed:25491382};
GN Name=sxy; Synonyms=tfoX {ECO:0000303|PubMed:19502395}, yccR;
GN OrderedLocusNames=b0959, JW0942;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
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 [3]
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 [4]
RP FUNCTION.
RX PubMed=17068078; DOI=10.1093/nar/gkl734;
RA Cameron A.D., Redfield R.J.;
RT "Non-canonical CRP sites control competence regulons in Escherichia coli
RT and many other gamma-proteobacteria.";
RL Nucleic Acids Res. 34:6001-6014(2006).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19502395; DOI=10.1128/jb.00476-09;
RA Sinha S., Cameron A.D., Redfield R.J.;
RT "Sxy induces a CRP-S regulon in Escherichia coli.";
RL J. Bacteriol. 191:5180-5195(2009).
RN [6]
RP FUNCTION.
RX PubMed=22532864; DOI=10.1371/journal.pone.0035620;
RA Sinha S., Redfield R.J.;
RT "Natural DNA uptake by Escherichia coli.";
RL PLoS ONE 7:E35620-E35620(2012).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076 {ECO:0000303|PubMed:25491382};
RX PubMed=25491382; DOI=10.1111/mmi.12901;
RA Jaskolska M., Gerdes K.;
RT "CRP-dependent positive autoregulation and proteolytic degradation regulate
RT competence activator Sxy of Escherichia coli.";
RL Mol. Microbiol. 95:833-845(2015).
CC -!- FUNCTION: Induces low levels of natural DNA uptake by inducing
CC transcription of the competence genes (the CRP-S regulon) required for
CC DNA transformation. Induction of the CRP-S regulon also requires Sxy-
CC activated promoter (CRP-S), cAMP receptor protein (CRP) and cAMP
CC (PubMed:17068078, PubMed:22532864). Induces CRP-S site-containing genes
CC which are involved in genome maintenance and transcription or encoding
CC transposases and toxin-antitoxin pairs (PubMed:19502395).
CC {ECO:0000269|PubMed:17068078, ECO:0000269|PubMed:19502395,
CC ECO:0000269|PubMed:22532864}.
CC -!- INTERACTION:
CC P75869; P75960: cobB; NbExp=9; IntAct=EBI-544452, EBI-544459;
CC P75869; P42184: prsA; Xeno; NbExp=2; IntAct=EBI-544452, EBI-544466;
CC -!- INDUCTION: Not expressed by conditions that usually induce expression
CC in other bacteria, such as amino acid starvation, antibiotics or
CC addition of chitin. Induces its own transcription by a mechanism that
CC requires CRP, cAMP and CRP-S site in its promoter. Negatively regulated
CC at the post-translational level via degradation by Lon protease.
CC {ECO:0000269|PubMed:25491382}.
CC -!- DISRUPTION PHENOTYPE: Reduces both natural plasmid transformation and
CC competitive fitness in long-term culture.
CC {ECO:0000269|PubMed:19502395}.
CC -!- MISCELLANEOUS: Overproduction induces the expression of the competence
CC regulon genes including ppdA, hofB and ssb, although to highly varying
CC degrees (PubMed:25491382). Plasmid-borne expression leads to production
CC of type IV pilin (T4P), the main subunit of the DNA uptake machinery
CC (PubMed:19502395). {ECO:0000269|PubMed:19502395,
CC ECO:0000269|PubMed:25491382}.
CC -!- SIMILARITY: Belongs to the TfoX family. {ECO:0000305}.
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DR EMBL; U00096; AAC74045.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35717.1; -; Genomic_DNA.
DR PIR; F64836; F64836.
DR RefSeq; NP_415479.1; NC_000913.3.
DR RefSeq; WP_000839153.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P75869; -.
DR SMR; P75869; -.
DR BioGRID; 4263154; 7.
DR BioGRID; 850853; 1.
DR DIP; DIP-11497N; -.
DR IntAct; P75869; 12.
DR STRING; 511145.b0959; -.
DR PaxDb; P75869; -.
DR PRIDE; P75869; -.
DR EnsemblBacteria; AAC74045; AAC74045; b0959.
DR EnsemblBacteria; BAA35717; BAA35717; BAA35717.
DR GeneID; 66670765; -.
DR GeneID; 946504; -.
DR KEGG; ecj:JW0942; -.
DR KEGG; eco:b0959; -.
DR PATRIC; fig|1411691.4.peg.1315; -.
DR EchoBASE; EB3484; -.
DR eggNOG; COG3070; Bacteria.
DR HOGENOM; CLU_094990_0_0_6; -.
DR OMA; AICGTHQ; -.
DR PhylomeDB; P75869; -.
DR BioCyc; EcoCyc:G6494-MON; -.
DR PRO; PR:P75869; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009290; P:DNA import into cell involved in transformation; IDA:UniProtKB.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:EcoCyc.
DR GO; GO:1903658; P:positive regulation of type IV pilus biogenesis; IDA:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IEP:UniProtKB.
DR InterPro; IPR007077; TfoX_C.
DR InterPro; IPR007076; TfoX_N.
DR InterPro; IPR026256; TfoX_Sxy.
DR Pfam; PF04994; TfoX_C; 1.
DR Pfam; PF04993; TfoX_N; 1.
DR PIRSF; PIRSF028788; TfoX_Sxy; 1.
PE 1: Evidence at protein level;
KW Activator; Competence; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..209
FT /note="Protein Sxy"
FT /id="PRO_0000168792"
SQ SEQUENCE 209 AA; 24147 MW; 588AD41143C4F2DA CRC64;
MKSLSYKRIY KSQEYLATLG TIEYRSLFGS YSLTVDDTVF AMVSDGELYL RACEQSAQYC
VKHPPVWLTY KKCGRSVTLN YYRVDESLWR NQLKLVRLSK YSLDAALKEK STRNTRERLK
DLPNMSFHLE AILGEVGIKD VRALRILGAK MCWLRLRQQN SLVTEKILFM LEGAIIGIHE
AALPVARRQE LAEWADSLTP KQEFPAELE
