ID   AIMR_BPPHT              Reviewed;         378 AA.
AC   P0DOE3;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 1.
DT   23-FEB-2022, entry version 24.
DE   RecName: Full=AimR transcriptional regulator {ECO:0000303|PubMed:28099413};
DE   AltName: Full=Arbitrium communication peptide receptor {ECO:0000303|PubMed:28099413};
GN   Name=aimR; OrderedLocusNames=phi3T_89;
OS   Bacillus phage phi3T (Bacteriophage phi-3T).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Spbetavirus; unclassified Spbetavirus.
OX   NCBI_TaxID=10736;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=28099413; DOI=10.1038/nature21049;
RA   Erez Z., Steinberger-Levy I., Shamir M., Doron S., Stokar-Avihail A.,
RA   Peleg Y., Melamed S., Leavitt A., Savidor A., Albeck S., Amitai G.,
RA   Sorek R.;
RT   "Communication between viruses guides lysis-lysogeny decisions.";
RL   Nature 541:488-493(2017).
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:0000269|PubMed:28099413}.
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:0000269|PubMed:28099413}.
CC   -!- DISRUPTION PHENOTYPE: Knockdown results in decreased AimX transcription
CC       and increased lysogeny. {ECO:0000269|PubMed:28099413}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Between you and me - Issue
CC       190 of April 2017;
CC       URL="https://web.expasy.org/spotlight/back_issues/190/";
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DR   EMBL; KY030782; APD21232.1; -; Genomic_DNA.
DR   PDB; 5ZVV; X-ray; 2.20 A; A/B=1-378.
DR   PDB; 5ZVW; X-ray; 2.29 A; A=1-378.
DR   PDBsum; 5ZVV; -.
DR   PDBsum; 5ZVW; -.
DR   SMR; P0DOE3; -.
DR   Proteomes; UP000188400; Genome.
DR   GO; GO:0098689; P:latency-replication decision; IDA:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   SUPFAM; SSF48452; SSF48452; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Latency-replication decision; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..378
FT                   /note="AimR transcriptional regulator"
FT                   /id="PRO_0000439256"
FT   HELIX           1..7
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           10..20
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           25..32
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           43..52
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           54..56
FT                   /evidence="ECO:0007829|PDB:5ZVW"
FT   HELIX           57..65
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           73..84
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           88..99
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           104..120
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           126..135
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           141..157
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           161..169
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           173..175
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           180..199
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           203..216
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           220..233
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   TURN            234..237
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           239..248
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           249..252
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           256..273
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           287..300
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           303..314
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           320..334
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           337..349
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           357..365
FT                   /evidence="ECO:0007829|PDB:5ZVV"
FT   HELIX           370..376
FT                   /evidence="ECO:0007829|PDB:5ZVV"
SQ   SEQUENCE   378 AA;  44107 MW;  053B37DF45FAC825 CRC64;
     MIKNECEKDN QLAARLAKLA GYEKVNGFYK FVNTPEKEME NLGGLLKIVK NLFPDSEEQL
     LSEYFLELDP NKKCARQSVE YSDINQWDTL TDKIIINLCN SKNSTSQEWG KVYSLHRKLN
     KNEISLNDAI RESGKCKIKS AEMLFFSNAM LMYAYLNIGE FGLMKSTSKL LEFDDLPEGF
     IKESFKSRVS MLEANISLNE NSLLEARQHS NRAIENSNVN RICFFAYLTI GNTLIFEDYD
     EAKKAYIKGQ KYAKNPVHQE MLDGALCFLS NIWKKENQWV NYNSDNIKYL QLRAFYYINQ
     GNIEEATEIL DELSSRDQDE NELGFYYYYK GLISQDKTDY YKSIRYFKKS DDKYFIQLPL
     LQLERMGADL ELLNLISI