ARCA_ECOLI
ID ARCA_ECOLI Reviewed; 238 AA.
AC P0A9Q1; P03026; Q2M5R6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Aerobic respiration control protein ArcA;
DE AltName: Full=Dye resistance protein;
GN Name=arcA; Synonyms=cpxC, dye, fexA, msp, seg, sfrA;
GN OrderedLocusNames=b4401, JW4364;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2984198; DOI=10.1016/s0021-9258(18)89255-9;
RA Drury L.S., Buxton R.S.;
RT "DNA sequence analysis of the dye gene of Escherichia coli reveals amino
RT acid homology between the dye and OmpR proteins.";
RL J. Biol. Chem. 260:4236-4242(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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 1-23.
RC STRAIN=K12;
RA Park S.J., Gunsalus R.P.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP PROTEIN SEQUENCE OF 40-45 AND 123-128, AND CHARACTERIZATION.
RX PubMed=7565118; DOI=10.1111/j.1365-2958.1995.tb02422.x;
RA Drapal N., Sawers G.;
RT "Purification of ArcA and analysis of its specific interaction with the pfl
RT promoter-regulatory region.";
RL Mol. Microbiol. 16:597-607(1995).
CC -!- FUNCTION: Member of the two-component regulatory system ArcB/ArcA.
CC Represses a wide variety of aerobic enzymes under anaerobic conditions.
CC Controls the resistance of E.coli to dyes; required for expression of
CC the alkaline phosphatase and sex factor F genes; It also may be
CC involved in the osmoregulation of envelope proteins. When activated by
CC ArcB, it negatively regulates the expression of genes of aerobic
CC function. Activates the transcription of the plfB operon by binding to
CC its promoter.
CC -!- INTERACTION:
CC P0A9Q1; P0A9Q1: arcA; NbExp=2; IntAct=EBI-1119939, EBI-1119939;
CC P0A9Q1; P52002: mexB; Xeno; NbExp=2; IntAct=EBI-1119939, EBI-6400435;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by ArcB.
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DR EMBL; M10044; AAA23718.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97297.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77354.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78390.1; -; Genomic_DNA.
DR EMBL; L34010; AAA23476.1; -; Genomic_DNA.
DR PIR; A03561; JYECR.
DR RefSeq; NP_418818.1; NC_000913.3.
DR RefSeq; WP_001194358.1; NZ_STEB01000033.1.
DR PDB; 1XHE; X-ray; 2.50 A; A/B=1-123.
DR PDB; 1XHF; X-ray; 2.15 A; A/B=1-123.
DR PDBsum; 1XHE; -.
DR PDBsum; 1XHF; -.
DR AlphaFoldDB; P0A9Q1; -.
DR SMR; P0A9Q1; -.
DR BioGRID; 4259386; 13.
DR DIP; DIP-36035N; -.
DR IntAct; P0A9Q1; 7.
DR STRING; 511145.b4401; -.
DR SWISS-2DPAGE; P0A9Q1; -.
DR jPOST; P0A9Q1; -.
DR PaxDb; P0A9Q1; -.
DR PRIDE; P0A9Q1; -.
DR EnsemblBacteria; AAC77354; AAC77354; b4401.
DR EnsemblBacteria; BAE78390; BAE78390; BAE78390.
DR GeneID; 67416078; -.
DR GeneID; 948874; -.
DR KEGG; ecj:JW4364; -.
DR KEGG; eco:b4401; -.
DR PATRIC; fig|1411691.4.peg.2283; -.
DR EchoBASE; EB0059; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_6; -.
DR InParanoid; P0A9Q1; -.
DR OMA; VWGWDFG; -.
DR PhylomeDB; P0A9Q1; -.
DR BioCyc; EcoCyc:ARCA-MON; -.
DR EvolutionaryTrace; P0A9Q1; -.
DR PHI-base; PHI:6532; -.
DR PRO; PR:P0A9Q1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR CollecTF; EXPREG_00000800; -.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032993; C:protein-DNA complex; IPI:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:EcoCyc.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IDA:EcoCyc.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:CollecTF.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:EcoCyc.
DR GO; GO:0000160; P:phosphorelay signal transduction system; 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; IDA:EcoCyc.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..238
FT /note="Aerobic respiration control protein ArcA"
FT /id="PRO_0000081008"
FT DOMAIN 5..118
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 134..234
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1XHF"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1XHF"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1XHF"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1XHF"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:1XHF"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1XHF"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1XHF"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:1XHF"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:1XHF"
FT HELIX 86..95
FT /evidence="ECO:0007829|PDB:1XHF"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:1XHF"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:1XHF"
SQ SEQUENCE 238 AA; 27292 MW; 9316CF4DE8EABDE8 CRC64;
MQTPHILIVE DELVTRNTLK SIFEAEGYDV FEATDGAEMH QILSEYDINL VIMDINLPGK
NGLLLARELR EQANVALMFL TGRDNEVDKI LGLEIGADDY ITKPFNPREL TIRARNLLSR
TMNLGTVSEE RRSVESYKFN GWELDINSRS LIGPDGEQYK LPRSEFRAML HFCENPGKIQ
SRAELLKKMT GRELKPHDRT VDVTIRRIRK HFESTPDTPE IIATIHGEGY RFCGDLED
