ID   ASIA_BPT4               Reviewed;          90 AA.
AC   P32267;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-JUN-2021, entry version 108.
DE   RecName: Full=10 kDa anti-sigma factor;
DE   AltName: Full=10 kDa RNA polymerase-associated protein;
DE   AltName: Full=Audrey Stevens' inhibitor;
GN   Name=asiA;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D;
RX   PubMed=8416914; DOI=10.1128/jb.175.1.85-93.1993;
RA   Orsini G., Ouhammouch M., Le Caer J.-P., Brody E.N.;
RT   "The asiA gene of bacteriophage T4 codes for the anti-sigma 70 protein.";
RL   J. Bacteriol. 175:85-93(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=8021178; DOI=10.1128/jb.176.13.3956-3965.1994;
RA   Ouhammouch M., Orsini G., Brody E.N.;
RT   "The asiA gene product of bacteriophage T4 is required for middle mode RNA
RT   synthesis.";
RL   J. Bacteriol. 176:3956-3965(1994).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=11518715; DOI=10.1074/jbc.m106400200;
RA   Urbauer J.L., Adelman K., Urbauer R.J., Simeonov M.F., Gilmore J.M.,
RA   Zolkiewski M., Brody E.N.;
RT   "Conserved regions 4.1 and 4.2 of sigma(70) constitute the recognition
RT   sites for the anti-sigma factor AsiA, and AsiA is a dimer free in
RT   solution.";
RL   J. Biol. Chem. 276:41128-41132(2001).
RN   [5]
RP   STRUCTURE BY NMR IN COMPLEX WITH HOST RPOD, AND FUNCTION.
RX   PubMed=15257291; DOI=10.1038/sj.emboj.7600312;
RA   Lambert L.J., Wei Y., Schirf V., Demeler B., Werner M.H.;
RT   "T4 AsiA blocks DNA recognition by remodeling sigma70 region 4.";
RL   EMBO J. 23:2952-2962(2004).
CC   -!- FUNCTION: Transcriptional inhibitor. Inhibits sigma 70-directed
CC       transcription by weakening its interaction with the core of the host's
CC       RNA polymerase. This allows Gp55 to successfully compete for the core
CC       enzyme. Plays an important role during the prereplicative period of
CC       phage T4 development. {ECO:0000269|PubMed:15257291,
CC       ECO:0000269|PubMed:8021178}.
CC   -!- SUBUNIT: Interacts with the host sigma factor RpoD, and thereby
CC       inhibits its interaction with the catalytic core of the host RNA
CC       polymerase. {ECO:0000269|PubMed:15257291}.
CC   -!- INTERACTION:
CC       P32267; P0A8V2: rpoB; Xeno; NbExp=4; IntAct=EBI-2124737, EBI-544996;
CC       P32267; P00579: rpoD; Xeno; NbExp=7; IntAct=EBI-2124737, EBI-545104;
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DR   EMBL; M99441; AAA32480.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42539.1; -; Genomic_DNA.
DR   RefSeq; NP_049866.1; NC_000866.4.
DR   PDB; 1JR5; NMR; -; A/B=1-90.
DR   PDB; 1TKV; NMR; -; A/B=1-90.
DR   PDB; 1TL6; NMR; -; A=1-90.
DR   PDB; 1TLH; NMR; -; A=1-90.
DR   PDB; 6K4Y; EM; 3.79 A; I=1-90.
DR   PDBsum; 1JR5; -.
DR   PDBsum; 1TKV; -.
DR   PDBsum; 1TL6; -.
DR   PDBsum; 1TLH; -.
DR   PDBsum; 6K4Y; -.
DR   BMRB; P32267; -.
DR   SMR; P32267; -.
DR   DIP; DIP-60748N; -.
DR   IntAct; P32267; 4.
DR   GeneID; 1258709; -.
DR   KEGG; vg:1258709; -.
DR   EvolutionaryTrace; P32267; -.
DR   Proteomes; UP000009087; Genome.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   Gene3D; 1.10.1810.10; -; 1.
DR   InterPro; IPR015100; AsiA.
DR   InterPro; IPR036486; AsiA_sf.
DR   Pfam; PF09010; AsiA; 1.
DR   SUPFAM; SSF69070; SSF69070; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..90
FT                   /note="10 kDa anti-sigma factor"
FT                   /id="PRO_0000164919"
FT   HELIX           4..20
FT                   /evidence="ECO:0007829|PDB:1JR5"
FT   HELIX           24..27
FT                   /evidence="ECO:0007829|PDB:1JR5"
FT   HELIX           30..40
FT                   /evidence="ECO:0007829|PDB:1JR5"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:1JR5"
FT   HELIX           52..59
FT                   /evidence="ECO:0007829|PDB:1JR5"
FT   HELIX           63..70
FT                   /evidence="ECO:0007829|PDB:1JR5"
FT   STRAND          73..77
FT                   /evidence="ECO:0007829|PDB:1JR5"
FT   TURN            78..82
FT                   /evidence="ECO:0007829|PDB:1JR5"
FT   HELIX           83..87
FT                   /evidence="ECO:0007829|PDB:1JR5"
SQ   SEQUENCE   90 AA;  10590 MW;  1802A150946F2D22 CRC64;
     MNKNIDTVRE IITVASILIK FSREDIVENR ANFIAFLNEI GVTHEGRKLN QNSFRKIVSE
     LTQEDKKTLI DEFNEGFEGV YRYLEMYTNK