ID   MATA2_BPMX1             Reviewed;         421 AA.
AC   O64306;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   23-FEB-2022, entry version 64.
DE   RecName: Full=Maturation protein A2;
DE            Short=MP;
DE   AltName: Full=A2;
DE   AltName: Full=Assembly protein;
DE            Short=A protein;
GN   Name=A;
OS   Escherichia phage Qbeta.
OC   Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC   Norzivirales; Fiersviridae; Qubevirus; Qubevirus durum.
OX   NCBI_TaxID=2789016;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=7723040; DOI=10.1006/jmbi.1995.0189;
RA   Beekwilder M.J., Nieuwenhuizen R., van Duin J.;
RT   "Secondary structure model for the last two domains of single-stranded RNA
RT   phage Q beta.";
RL   J. Mol. Biol. 247:903-917(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8609616; DOI=10.1006/jmbi.1996.0064;
RA   Beekwilder J., Nieuwenhuizen R., Poot R., van Duin J.;
RT   "Secondary structure model for the first three domains of Q beta RNA.
RT   Control of A-protein synthesis.";
RL   J. Mol. Biol. 256:8-19(1996).
CC   -!- FUNCTION: Induces host cell lysis. Inhibits host MurA activity thereby
CC       blocking the synthesis of murein precursors necessary for the host cell
CC       wall biosynthesis. May be responsible for the attachment to the host
CC       pilus. {ECO:0000250|UniProtKB:Q8LTE2}.
CC   -!- SUBUNIT: Interacts with host MurA; this interaction inhibits the first
CC       step in host cell wall synthesis. Interacts with the capsid protein
CC       dimers. {ECO:0000250|UniProtKB:Q8LTE2}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:Q8LTE2}. Note=A
CC       single copy of the maturation protein is present in the virion.
CC       {ECO:0000250|UniProtKB:Q8LTE2}.
CC   -!- SIMILARITY: Belongs to the Levivirus maturation protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF059242; AAC14698.1; -; Genomic_RNA.
DR   RefSeq; NP_046749.1; NC_001890.1.
DR   SMR; O64306; -.
DR   GeneID; 1261501; -.
DR   KEGG; vg:1261501; -.
DR   Proteomes; UP000001832; Genome.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0039666; P:virion attachment to host cell pilus; IEA:UniProtKB-KW.
DR   InterPro; IPR005563; A_protein.
DR   Pfam; PF03863; Phage_mat-A; 1.
PE   3: Inferred from homology;
KW   Cytolysis; Host cell lysis by virus; Host-virus interaction;
KW   Reference proteome; RNA-binding;
KW   Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW   Viral attachment to host cell pilus; Viral release from host cell; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..421
FT                   /note="Maturation protein A2"
FT                   /id="PRO_0000402540"
FT   REGION          159..177
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LTE2"
FT   REGION          227..237
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LTE2"
FT   REGION          295..299
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q8LTE2"
SQ   SEQUENCE   421 AA;  48486 MW;  3978CB9E7E9D0943 CRC64;
     MPRLPRALRF GPNMEVLSDF QELWYPESII DSDVKYPLYT FRGSIGGSFF DSYGTNNIVR
     EIRRTPHCAT VPIASSGLRP CTSVWYDPTS LLFRIPEMRA EWDNGMGDAG DIVYKDFLFS
     TPAPKEFDFS NSLAPRYSNA FSAFNAKYGV IIGEGHETLK YFALLLRRLH KAVRAVRHGD
     LRGLRKILDS YNKGRWKPAT AGNLWLEFRY GLTPLFHDIK SVMDDWNRIN DKIQKLRRFS
     VGHGEDFKLS IDGLYPGLTH FRLSGEITVQ RRHRWGITYA NREGYATFDN GSIRPVSDWK
     ELANAFINPG EVAWELTPYS FIVDWFINVG DIIEQQKQWY QNIDIVDGYQ RRDIRMRSVS
     LKGVRNGIPV RVTGSVELVD SFYNRSHTTR IPQATLAIDT SFSSIKHVMD SISLITQRIK
     R