ASNC_ECOLI
ID ASNC_ECOLI Reviewed; 152 AA.
AC P0ACI6; P03809; Q2M861;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Regulatory protein AsnC;
GN Name=asnC; OrderedLocusNames=b3743, JW3721;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6117826; DOI=10.1093/nar/9.18.4669;
RA Nakamura M., Yamada M., Hirota Y., Sugimoto K., Oka A., Takanami M.;
RT "Nucleotide sequence of the asnA gene coding for asparagine synthetase of
RT E. coli K-12.";
RL Nucleic Acids Res. 9:4669-4676(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6357950; DOI=10.1016/0378-1119(83)90087-2;
RA Buhk H.-J., Messer W.;
RT "The replication origin region of Escherichia coli: nucleotide sequence and
RT functional units.";
RL Gene 24:265-279(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=3909107; DOI=10.1093/nar/13.24.8797;
RA de Wind N., de Jong M., Meijer M., Stuitje A.R.;
RT "Site-directed mutagenesis of the Escherichia coli chromosome near oriC:
RT identification and characterization of asnC, a regulatory element in E.
RT coli asparagine metabolism.";
RL Nucleic Acids Res. 13:8797-8811(1985).
RN [7]
RP FUNCTION.
RX PubMed=2864330; DOI=10.1128/jb.164.1.310-315.1985;
RA Koelling R., Lother H.;
RT "AsnC: an autogenously regulated activator of asparagine synthetase A
RT transcription in Escherichia coli.";
RL J. Bacteriol. 164:310-315(1985).
RN [8]
RP FUNCTION.
RX PubMed=2836709; DOI=10.1007/bf00322450;
RA Koelling R., Gielow A., Seufert W., Kuecherer C., Messer W.;
RT "AsnC, a multifunctional regulator of genes located around the replication
RT origin of Escherichia coli, oriC.";
RL Mol. Gen. Genet. 212:99-104(1988).
CC -!- FUNCTION: Activator of asnA transcription; autogenous regulator of its
CC own transcription; and repressor of the expression of gidA at a post-
CC transcriptional level. {ECO:0000269|PubMed:2836709,
CC ECO:0000269|PubMed:2864330, ECO:0000269|PubMed:3909107}.
CC -!- INTERACTION:
CC P0ACI6; P31658: hchA; NbExp=2; IntAct=EBI-1133670, EBI-909144;
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; V00263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; K00826; AAA24252.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62095.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76766.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77545.1; -; Genomic_DNA.
DR PIR; A04434; QQECE1.
DR RefSeq; NP_418199.1; NC_000913.3.
DR RefSeq; WP_000432970.1; NZ_STEB01000015.1.
DR RefSeq; YP_006952152.1; NC_019049.1.
DR PDB; 2CG4; X-ray; 2.40 A; A/B=1-152.
DR PDBsum; 2CG4; -.
DR AlphaFoldDB; P0ACI6; -.
DR SMR; P0ACI6; -.
DR BioGRID; 4263262; 98.
DR BioGRID; 852561; 1.
DR DIP; DIP-9178N; -.
DR IntAct; P0ACI6; 1.
DR STRING; 511145.b3743; -.
DR jPOST; P0ACI6; -.
DR PaxDb; P0ACI6; -.
DR PRIDE; P0ACI6; -.
DR EnsemblBacteria; AAC76766; AAC76766; b3743.
DR EnsemblBacteria; BAE77545; BAE77545; BAE77545.
DR GeneID; 67417730; -.
DR GeneID; 948259; -.
DR KEGG; ecj:JW3721; -.
DR KEGG; eco:b3743; -.
DR PATRIC; fig|1411691.4.peg.2957; -.
DR EchoBASE; EB0091; -.
DR eggNOG; COG1522; Bacteria.
DR HOGENOM; CLU_091233_5_0_6; -.
DR InParanoid; P0ACI6; -.
DR OMA; EDCWFIA; -.
DR PhylomeDB; P0ACI6; -.
DR BioCyc; EcoCyc:PD00250; -.
DR EvolutionaryTrace; P0ACI6; -.
DR PRO; PR:P0ACI6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
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:0043200; P:response to amino acid; IDA:EcoCyc.
DR CDD; cd00090; HTH_ARSR; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011991; ArsR-like_HTH.
DR InterPro; IPR000485; AsnC-type_HTH_dom.
DR InterPro; IPR011008; Dimeric_a/b-barrel.
DR InterPro; IPR019888; Tscrpt_reg_AsnC-like.
DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C.
DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01037; AsnC_trans_reg; 1.
DR PRINTS; PR00033; HTHASNC.
DR SMART; SM00344; HTH_ASNC; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF54909; SSF54909; 1.
DR PROSITE; PS00519; HTH_ASNC_1; 1.
DR PROSITE; PS50956; HTH_ASNC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..152
FT /note="Regulatory protein AsnC"
FT /id="PRO_0000111719"
FT DOMAIN 6..67
FT /note="HTH asnC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT DNA_BIND 25..44
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00319"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:2CG4"
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:2CG4"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:2CG4"
FT STRAND 51..59
FT /evidence="ECO:0007829|PDB:2CG4"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:2CG4"
FT STRAND 68..78
FT /evidence="ECO:0007829|PDB:2CG4"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2CG4"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2CG4"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:2CG4"
FT STRAND 106..114
FT /evidence="ECO:0007829|PDB:2CG4"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:2CG4"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:2CG4"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:2CG4"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2CG4"
SQ SEQUENCE 152 AA; 16888 MW; B37581D88D15ECED CRC64;
MENYLIDNLD RGILEALMGN ARTAYAELAK QFGVSPGTIH VRVEKMKQAG IITGARIDVS
PKQLGYDVGC FIGIILKSAK DYPSALAKLE SLDEVTEAYY TTGHYSIFIK VMCRSIDALQ
HVLINKIQTI DEIQSTETLI VLQNPIMRTI KP
