MATA_BPMS2
ID MATA_BPMS2 Reviewed; 393 AA.
AC P03610;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Maturation protein A;
DE Short=MP;
DE AltName: Full=Assembly protein;
DE Short=A protein;
GN Name=A;
OS Escherichia phage MS2 (Bacteriophage MS2).
OC Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC Levivirales; Leviviridae; Levivirus.
OX NCBI_TaxID=329852;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=806810; DOI=10.1038/256273a0;
RA Fiers W., Contreras R., Duerinck F., Haegeman G., Merregaert J.,
RA Min Jou W., Raeymaekers A., Volckaert G., Ysebaert M., Vandekerckhove J.,
RA Nolf F., van Montagu M.;
RT "A-protein gene of bacteriophage MS2.";
RL Nature 256:273-278(1975).
RN [2]
RP PROTEIN SEQUENCE.
RX PubMed=914838; DOI=10.1016/s0021-9258(17)41034-9;
RA Vandekerckhove J., van Montagu M.;
RT "Sequence of the A-protein of coliphage MS2. III. Isolation and sequence
RT determination of thermolytic peptides and soluble cyanogen bromide
RT fragments: alignment of 363 amino acid residues of a total of 393.";
RL J. Biol. Chem. 252:7773-7782(1977).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 350-393.
RX PubMed=4512458; DOI=10.1038/newbio241099a0;
RA Contreras R.R., Ysebaert M., Jou W.M., Fiers W.;
RT "Bacteriophage Ms2 RNA: nucleotide sequence of the end of the a protein
RT gene and the intercistronic region.";
RL Nature New Biol. 241:99-101(1973).
RN [4]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=914837; DOI=10.1016/s0021-9258(17)41033-7;
RA Vandekerckhove J., Gielen J.G., van Montagu M.;
RT "Sequence of the A-protein of coliphage MS2. II. Isolation and sequence
RT determination of chymotryptic peptides.";
RL J. Biol. Chem. 252:7761-7772(1977).
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=914836; DOI=10.1016/s0021-9258(17)41032-5;
RA Nolf F., Vandekerckhove J., Lenaerts A.K., van Montagu M.;
RT "Sequence of the A-protein of coliphage MS2. I. Isolation of A-protein,
RT determination of the NH2- and COOH-terminal sequences, isolation and amino
RT acid sequence of the tryptic peptides.";
RL J. Biol. Chem. 252:7752-7760(1977).
RN [6]
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=4551992; DOI=10.1016/0042-6822(72)90552-1;
RA Krahn P.M., O'Callaghan R.J., Paranchych W.;
RT "Stages in phage R17 infection. VI. Injection of A protein and RNA into the
RT host cell.";
RL Virology 47:628-637(1972).
RN [7]
RP RNA-BINDING.
RX PubMed=6974569; DOI=10.1016/0005-2787(81)90179-9;
RA Shiba T., Suzuki Y.;
RT "Localization of A protein in the RNA-A protein complex of RNA phage MS2.";
RL Biochim. Biophys. Acta 654:249-255(1981).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH THE HOST PILUS.
RX PubMed=23810697; DOI=10.1016/j.str.2013.05.012;
RA Dent K.C., Thompson R., Barker A.M., Hiscox J.A., Barr J.N., Stockley P.G.,
RA Ranson N.A.;
RT "The asymmetric structure of an icosahedral virus bound to its receptor
RT suggests a mechanism for genome release.";
RL Structure 21:1225-1234(2013).
RN [9]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=26608810; DOI=10.1016/j.jmb.2015.11.014;
RA Rolfsson O., Middleton S., Manfield I.W., White S.J., Fan B., Vaughan R.,
RA Ranson N.A., Dykeman E., Twarock R., Ford J., Kao C.C., Stockley P.G.;
RT "Direct evidence for packaging signal-mediated assembly of bacteriophage
RT MS2.";
RL J. Mol. Biol. 428:431-448(2016).
CC -!- FUNCTION: The maturation protein is required for the typical attachment
CC of the phage to the side of the bacterial pili (PubMed:23810697). Binds
CC to sequences located toward each end of the genome, hence circularizing
CC it (PubMed:26608810). The RNA genome-maturation protein A complex is
CC released from the capsid upon host receptor binding (PubMed:23810697).
CC Maturation protein A enters the cell along with the viral RNA
CC (PubMed:4551992). {ECO:0000269|PubMed:23810697,
CC ECO:0000269|PubMed:26608810, ECO:0000269|PubMed:4551992}.
CC -!- SUBUNIT: Interacts with the host pilus. {ECO:0000269|PubMed:23810697}.
CC -!- SUBCELLULAR LOCATION: Virion. Note=A single copy of the maturation
CC protein is present in the virion. {ECO:0000305|PubMed:23810697}.
CC -!- PTM: During internalization, MP is proteolytically cleaved into two
CC fragments allowing translation and replication to start.
CC {ECO:0000269|PubMed:4551992}.
CC -!- SIMILARITY: Belongs to the Levivirus maturation protein family.
CC {ECO:0000305}.
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DR EMBL; V00642; CAA23988.1; -; mRNA.
DR EMBL; M25187; AAA32257.1; -; Genomic_RNA.
DR PIR; A93176; ACBPMS.
DR RefSeq; NP_040647.1; NC_001417.2.
DR PDB; 5TC1; EM; 3.60 A; M=1-393.
DR PDB; 6NM5; EM; 6.20 A; M=1-393.
DR PDBsum; 5TC1; -.
DR PDBsum; 6NM5; -.
DR SMR; P03610; -.
DR PRIDE; P03610; -.
DR Proteomes; UP000002127; Genome.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0099009; P:viral genome circularization; IEA:UniProtKB-KW.
DR GO; GO:0039666; P:virion attachment to host cell pilus; IDA:UniProtKB.
DR InterPro; IPR005563; A_protein.
DR Pfam; PF03863; Phage_mat-A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Host-virus interaction;
KW Reference proteome; RNA-binding; Viral attachment to host cell;
KW Viral attachment to host cell pilus; Viral genome circularization;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT CHAIN 1..393
FT /note="Maturation protein A"
FT /id="PRO_0000164859"
FT REGION 26..233
FT /note="Viral RNA-binding"
FT /evidence="ECO:0000269|PubMed:26608810"
SQ SEQUENCE 393 AA; 43983 MW; A596DB35F08F80CC CRC64;
MRAFSTLDRE NETFVPSVRV YADGETEDNS FSLKYRSNWT PGRFNSTGAK TKQWHYPSPY
SRGALSVTSI DQGAYKRSGS SWGRPYEEKA GFGFSLDARS CYSLFPVSQN LTYIEVPQNV
ANRASTEVLQ KVTQGNFNLG VALAEARSTA SQLATQTIAL VKAYTAARRG NWRQALRYLA
LNEDRKFRSK HVAGRWLELQ FGWLPLMSDI QGAYEMLTKV HLQEFLPMRA VRQVGTNIKL
DGRLSYPAAN FQTTCNISRR IVIWFYINDA RLAWLSSLGI LNPLGIVWEK VPFSFVVDWL
LPVGNMLEGL TAPVGCSYMS GTVTDVITGE SIISVDAPYG WTVERQGTAK AQISAMHRGV
QSVWPTTGAY VKSPFSMVHT LDALALIRQR LSR
