YEIL_ECO57
ID YEIL_ECO57 Reviewed; 219 AA.
AC P0A9F0; P33023;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Regulatory protein YeiL;
GN Name=yeiL; OrderedLocusNames=Z3420, ECs3055;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Transcription regulator involved in mid-term, stationary-
CC phase viability under nitrogen starvation. Might control expression of
CC the salvage pathways or in some other way repress the recycling of
CC nucleobases to nucleic acids and enhance their use as general nitrogen
CC sources during nitrogen-limited growth (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000305};
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005174; AAG57301.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36478.1; -; Genomic_DNA.
DR PIR; A85855; A85855.
DR PIR; G91010; G91010.
DR RefSeq; NP_311082.3; NC_002695.1.
DR RefSeq; WP_001310375.1; NZ_SEKU01000013.1.
DR AlphaFoldDB; P0A9F0; -.
DR SMR; P0A9F0; -.
DR STRING; 155864.EDL933_3327; -.
DR EnsemblBacteria; AAG57301; AAG57301; Z3420.
DR EnsemblBacteria; BAB36478; BAB36478; ECs_3055.
DR GeneID; 916759; -.
DR KEGG; ece:Z3420; -.
DR KEGG; ecs:ECs_3055; -.
DR PATRIC; fig|386585.9.peg.3184; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_075053_11_1_6; -.
DR OMA; TSNVQVM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 1.
DR SMART; SM00100; cNMP; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; Activator; Cytoplasm; DNA-binding; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..219
FT /note="Regulatory protein YeiL"
FT /id="PRO_0000100183"
FT DOMAIN 136..199
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 158..181
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT REGION 19..97
FT /note="Sensory domain"
FT /evidence="ECO:0000255"
FT REGION 111..131
FT /note="Dimer interface"
FT /evidence="ECO:0000255"
FT BINDING 68
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 91
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 93
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 116
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 219 AA; 25294 MW; 47720B07A9FD412D CRC64;
MSESAFKDCF LTDVSADTRL FHFLARDYIV QEGQQPSWLF YLTRGRARLY ATLANGRVSL
IDFFAAPCFI GEIELIDKDH EPRAVQAIEE CWCLALPMKH YRPLLLNDTL FLRKLCVTLS
HKNYRNIVSL TQNQSFPLVN RLAAFILLSQ EGDLYHEKHT QAAEYLGVSY RHLLYVLAQF
IHDGLLIKSK KGYLIKNRKQ LSGLALEMDP ENKFSGMMQ
