AIMR_BPSPB
ID AIMR_BPSPB Reviewed; 386 AA.
AC O64094;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 02-JUN-2021, entry version 63.
DE RecName: Full=AimR transcriptional regulator {ECO:0000250|UniProtKB:P0DOE3};
DE AltName: Full=Arbitrium communication peptide receptor {ECO:0000250|UniProtKB:P0DOE3};
DE AltName: Full=YopK protein;
GN Name=aimR {ECO:0000250|UniProtKB:P0DOE3}; Synonyms=yopK;
OS Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Spbetavirus.
OX NCBI_TaxID=66797;
OH NCBI_TaxID=1408; Bacillus pumilus (Bacillus mesentericus).
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9465078; DOI=10.1073/pnas.95.4.1692;
RA Lazarevic V., Soldo B., Duesterhoeft A., Hilbert H., Maueel C.,
RA Karamata D.;
RT "Introns and intein coding sequence in the ribonucleotide reductase genes
RT of Bacillus subtilis temperate bacteriophage SPbeta.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1692-1697(1998).
CC -!- FUNCTION: Transcriptional regulator which is part of the latency-
CC replication switch system that decides at the onset of infection
CC whether to replicate and lyse the host or to lysogenize (latency) and
CC keep the host viable. Activates the transcription of the aimX locus.
CC Transcriptional activation of aimX seems to lead to the productive
CC viral replication (lytic cycle), aimX possibly acting as a regulatory
CC non-coding RNA. {ECO:0000250|UniProtKB:P0DOE3}.
CC -!- SUBUNIT: Homodimer. Interacts with the viral arbitrium peptide, this
CC interaction changes the oligomeric state of AimR from an active dimer
CC to an inactive monomer leading to lysogeny.
CC {ECO:0000250|UniProtKB:P0DOE3}.
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DR EMBL; AF020713; AAC13054.1; -; Genomic_DNA.
DR PIR; T12845; T12845.
DR RefSeq; NP_046633.1; NC_001884.1.
DR PDB; 5XYB; X-ray; 2.20 A; A/B=1-386.
DR PDB; 5Y24; X-ray; 1.92 A; A/B=1-386.
DR PDB; 5ZW5; X-ray; 2.40 A; A/B=1-386.
DR PDB; 5ZW6; X-ray; 2.05 A; A/B=1-386.
DR PDB; 6IM4; X-ray; 1.93 A; A/B=1-386.
DR PDB; 6IPX; X-ray; 2.63 A; A/B=1-386.
DR PDB; 6JG5; X-ray; 2.22 A; A/B=1-386.
DR PDB; 6JG8; X-ray; 2.10 A; A/B=1-386.
DR PDB; 6JG9; X-ray; 2.00 A; A/B=1-386.
DR PDBsum; 5XYB; -.
DR PDBsum; 5Y24; -.
DR PDBsum; 5ZW5; -.
DR PDBsum; 5ZW6; -.
DR PDBsum; 6IM4; -.
DR PDBsum; 6IPX; -.
DR PDBsum; 6JG5; -.
DR PDBsum; 6JG8; -.
DR PDBsum; 6JG9; -.
DR SMR; O64094; -.
DR GeneID; 1261404; -.
DR KEGG; vg:1261404; -.
DR Proteomes; UP000009091; Genome.
DR GO; GO:0098689; P:latency-replication decision; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Latency-replication decision; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..386
FT /note="AimR transcriptional regulator"
FT /id="PRO_0000439257"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:6IM4"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:6IM4"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6IM4"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:6IM4"
FT HELIX 49..58
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 110..126
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 132..142
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 147..163
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 186..206
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:5Y24"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 246..260
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 264..280
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 295..307
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 311..321
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 328..342
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 345..358
FT /evidence="ECO:0007829|PDB:5Y24"
FT TURN 361..364
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 365..373
FT /evidence="ECO:0007829|PDB:5Y24"
FT HELIX 378..386
FT /evidence="ECO:0007829|PDB:5Y24"
SQ SEQUENCE 386 AA; 45320 MW; 3C341F5D43A0CDE1 CRC64;
MELIRIAMKK DLENDNSLMN KWATVAGLKN PNPLYDFLNH DGKTFNEFSS IVNIVKSQYP
DREYELMKDY CLNLDVKTKA ARSALEYADA NMFFEIEDVL IDSMISCSNM KSKEYGKVYK
IHRELSNSVI TEFEAVKRLG KLNIKTPEMN SFSRLLLLYH YLSTGNFSPM AQLIKQIDLS
EISENMYIRN TYQTRVHVLM SNIKLNENSL EECREYSKKA LESTNILRFQ VFSYLTIGNS
LLFSNYELAQ ENFLKGLSIS VQNENYNMIF QQALCFLNNV WRKENKWINF ESDSIMDLQE
QAHCFINFNE NSKAKEVLDK LDLLVHNDNE LAMHYYLKGR LEQNKACFYS SIEYFKKSND
KFLIRLPLLE LQKMGENQKL LELLLL
