MATA2_BPQBE
ID MATA2_BPQBE Reviewed; 420 AA.
AC Q8LTE2; C8YJH8; D0U1F1; D0U1F5; D0U1F9; D0U1G3; G4WZR1; G4WZR5;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Maturation protein A2 {ECO:0000312|EMBL:AAM33125.1};
DE Short=MP;
DE AltName: Full=A2 protein;
OS Escherichia virus Qbeta (Bacteriophage Q-beta).
OC Viruses; Riboviria; Orthornavirae; Lenarviricota; Leviviricetes;
OC Levivirales; Leviviridae; Allolevivirus.
OX NCBI_TaxID=39803 {ECO:0000312|EMBL:AAM33125.1};
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=14667253; DOI=10.1186/1471-2148-3-24;
RA Bacher J.M., Bull J.J., Ellington A.D.;
RT "Evolution of phage with chemically ambiguous proteomes.";
RL BMC Evol. Biol. 3:24-24(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=TW18 {ECO:0000312|EMBL:ACT66729.1,
RC ECO:0000312|Proteomes:UP000001616};
RX PubMed=19710143; DOI=10.1128/jvi.01308-09;
RA Friedman S.D., Genthner F.J., Gentry J., Sobsey M.D., Vinje J.;
RT "Gene mapping and phylogenetic analysis of the complete genome from 30
RT single-stranded RNA male-specific coliphages (family Leviviridae).";
RL J. Virol. 83:11233-11243(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=QB_1 {ECO:0000312|EMBL:ACY07222.1},
RC QB_2 {ECO:0000312|EMBL:ACY07226.1}, QB_3 {ECO:0000312|EMBL:ACY07230.1}, and
RC QB_ancestral {ECO:0000312|EMBL:ACY07234.1};
RX PubMed=19956760; DOI=10.1371/journal.pgen.1000742;
RA Domingo-Calap P., Cuevas J.M., Sanjuan R.;
RT "The fitness effects of random mutations in single-stranded DNA and RNA
RT bacteriophages.";
RL PLoS Genet. 5:E1000742-E1000742(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Qbeta_1_FR {ECO:0000312|EMBL:AEQ25540.1},
RC Qbeta_2_FR {ECO:0000312|EMBL:AEQ25544.1}, and
RC Qbeta_3_FR {ECO:0000312|EMBL:AEQ25548.1};
RX PubMed=21967437; DOI=10.1111/j.1558-5646.2011.01339.x;
RA Domingo-Calap P., Sanjuan R.;
RT "Experimental evolution of RNA versus DNA viruses.";
RL Evolution 65:2987-2994(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=QB_ancestral {ECO:0000312|EMBL:BAP18762.1}, and
RC TW18 {ECO:0000312|Proteomes:UP000001616};
RX PubMed=25056887; DOI=10.1128/jvi.01127-14;
RA Kashiwagi A., Sugawara R., Sano-Tsushima F., Kumagai T., Yomo T.;
RT "Contribution of silent mutations to thermal adaptation of RNA
RT bacteriophage Qbeta.";
RL J. Virol. 88:11459-11468(2014).
RN [6]
RP FUNCTION.
RX PubMed=11892805; DOI=10.1002/j.1460-2075.1983.tb01617.x;
RA Karnik S., Billeter M.;
RT "The lysis function of RNA bacteriophage Qbeta is mediated by the
RT maturation (A2) protein.";
RL EMBO J. 2:1521-1526(1983).
RN [7]
RP FUNCTION.
RX PubMed=11423662; DOI=10.1126/science.1058289;
RA Bernhardt T.G., Wang I.N., Struck D.K., Young R.;
RT "A protein antibiotic in the phage Qbeta virion: diversity in lysis
RT targets.";
RL Science 292:2326-2329(2001).
RN [8]
RP INTERACTION WITH HOST MURA.
RX PubMed=22934834; DOI=10.1111/mmi.12021;
RA Reed C.A., Langlais C., Kuznetsov V., Young R.;
RT "Inhibitory mechanism of the Qbeta lysis protein A2.";
RL Mol. Microbiol. 86:836-844(2012).
RN [9]
RP FUNCTION.
RX PubMed=23329676; DOI=10.1099/mic.0.064790-0;
RA Reed C.A., Langlais C., Wang I.N., Young R.;
RT "A(2) expression and assembly regulates lysis in Qbeta infections.";
RL Microbiology 159:507-514(2013).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=27671640; DOI=10.1073/pnas.1609482113;
RA Gorzelnik K.V., Cui Z., Reed C.A., Jakana J., Young R., Zhang J.;
RT "Asymmetric cryo-EM structure of the canonical Allolevivirus Qbeta reveals
RT a single maturation protein and the genomic ssRNA in situ.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:11519-11524(2016).
RN [11] {ECO:0007744|PDB:5MNT}
RP X-RAY CRYSTALLOGRAPHY (3.32 ANGSTROMS) OF 2-420, RNA-BINDING, AND
RP INTERACTION WITH CAPSID PROTEIN.
RX PubMed=28111107; DOI=10.1016/j.jmb.2017.01.012;
RA Rumnieks J., Tars K.;
RT "Crystal structure of the maturation protein from bacteriophage Qbeta.";
RL J. Mol. Biol. 429:688-696(2017).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.40 ANGSTROMS), INTERACTION WITH HOST
RP MURA, INTERACTION WITH THE CAPSID PROTEIN, FUNCTION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=29078304; DOI=10.1073/pnas.1707102114;
RA Cui Z., Gorzelnik K.V., Chang J.Y., Langlais C., Jakana J., Young R.,
RA Zhang J.;
RT "Structures of Qbeta virions, virus-like particles, and the Qbeta-MurA
RT complex reveal internal coat proteins and the mechanism of host lysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:11697-11702(2017).
CC -!- FUNCTION: Induces host cell lysis (PubMed:11892805, PubMed:29078304).
CC Inhibits host MurA activity thereby blocking the synthesis of murein
CC precursors necessary for the host cell wall biosynthesis
CC (PubMed:11423662, PubMed:29078304). May be responsible for the
CC attachment to the host pilus. Makes extensive contacts with the viral
CC genome (PubMed:28111107). {ECO:0000269|PubMed:11423662,
CC ECO:0000269|PubMed:11892805, ECO:0000269|PubMed:23329676,
CC ECO:0000269|PubMed:28111107, ECO:0000269|PubMed:29078304}.
CC -!- SUBUNIT: Interacts with host MurA; this interaction inhibits the first
CC step in host cell wall synthesis (PubMed:22934834, PubMed:29078304).
CC Interacts with the capsid protein (PubMed:28111107, PubMed:29078304).
CC {ECO:0000269|PubMed:22934834, ECO:0000269|PubMed:28111107,
CC ECO:0000269|PubMed:29078304}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27671640,
CC ECO:0000269|PubMed:29078304}. Note=A single copy of the maturation
CC protein is present in the virion. {ECO:0000269|PubMed:27671640,
CC ECO:0000269|PubMed:29078304}.
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DR EMBL; AY099114; AAM33125.1; -; Genomic_RNA.
DR EMBL; FJ483840; ACT66729.1; -; Genomic_RNA.
DR EMBL; GQ153928; ACY07222.1; -; Genomic_RNA.
DR EMBL; GQ153929; ACY07226.1; -; Genomic_RNA.
DR EMBL; GQ153930; ACY07230.1; -; Genomic_RNA.
DR EMBL; GQ153931; ACY07234.1; -; Genomic_RNA.
DR EMBL; JF719735; AEQ25540.1; -; Genomic_RNA.
DR EMBL; JF719736; AEQ25544.1; -; Genomic_RNA.
DR EMBL; JF719737; AEQ25548.1; -; Genomic_RNA.
DR EMBL; AB971354; BAP18762.1; -; Genomic_RNA.
DR PDB; 5MNT; X-ray; 3.32 A; A/B/C/D=2-420.
DR PDB; 5VLZ; EM; 4.40 A; EJ=1-420.
DR PDB; 5VM7; EM; 5.70 A; A=1-420.
DR PDB; 7LHD; EM; 4.60 A; M=1-420.
DR PDBsum; 5MNT; -.
DR PDBsum; 5VLZ; -.
DR PDBsum; 5VM7; -.
DR PDBsum; 7LHD; -.
DR SMR; Q8LTE2; -.
DR Proteomes; UP000001616; Genome.
DR Proteomes; UP000185268; Genome.
DR Proteomes; UP000305125; Genome.
DR Proteomes; UP000306921; Genome.
DR Proteomes; UP000309733; Genome.
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:0039636; P:suppression by virus of host cell wall biogenesis; IDA:UniProtKB.
DR GO; GO:0039635; P:suppression by virus of host peptidoglycan biosynthetic process; IDA:CACAO.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0039640; P:viral release by cytolysis via suppression of host peptidoglycan biosynthetic process; IDA:CACAO.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IMP:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Host cell lysis by virus; Host-virus interaction;
KW Reference proteome; Viral attachment to host adhesion receptor;
KW Viral attachment to host cell; Viral attachment to host cell pilus;
KW Viral release from host cell; Virion; Virus entry into host cell.
FT CHAIN 1..420
FT /note="Maturation protein A2"
FT /id="PRO_0000438881"
FT REGION 158..176
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:28111107"
FT REGION 226..236
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:28111107"
FT REGION 294..298
FT /note="RNA-binding"
FT /evidence="ECO:0000269|PubMed:28111107"
FT VARIANT 29
FT /note="F -> L (in strain: Qbeta_2_FR)"
FT /evidence="ECO:0000269|PubMed:21967437"
FT VARIANT 76
FT /note="S -> L (in strain: Qbeta_2)"
FT /evidence="ECO:0000269|PubMed:19956760"
FT VARIANT 100
FT /note="D -> G (in strain: Qbeta_2)"
FT /evidence="ECO:0000269|PubMed:19956760"
FT VARIANT 110
FT /note="N -> D (in strain: Qbeta_2_FR)"
FT /evidence="ECO:0000269|PubMed:21967437"
FT VARIANT 121
FT /note="F -> S (in strain: TW18)"
FT /evidence="ECO:0000269|PubMed:19710143"
FT VARIANT 138
FT /note="Q -> K (in strain: Qbeta_3_FR)"
FT /evidence="ECO:0000269|PubMed:21967437"
FT VARIANT 189
FT /note="S -> F (in strain: Qbeta_3)"
FT /evidence="ECO:0000269|PubMed:19956760"
FT VARIANT 198
FT /note="A -> T (in strain: TW18)"
FT /evidence="ECO:0000269|PubMed:19710143"
FT VARIANT 218
FT /note="I -> V (in strain: Qbeta_3_FR)"
FT /evidence="ECO:0000269|PubMed:21967437"
FT VARIANT 219
FT /note="R -> G (in strain: Qbeta_1)"
FT /evidence="ECO:0000269|PubMed:19956760"
FT VARIANT 219
FT /note="R -> K (in strain: TW18)"
FT /evidence="ECO:0000269|PubMed:19710143"
FT VARIANT 246
FT /note="Y -> C (in strain: TW18)"
FT /evidence="ECO:0000269|PubMed:19710143"
FT VARIANT 254
FT /note="Y -> C (in strain: Qbeta_3)"
FT /evidence="ECO:0000269|PubMed:19956760"
FT VARIANT 282
FT /note="E -> G (in strain: Qbeta_3_FR and Qbeta_3)"
FT /evidence="ECO:0000269|PubMed:19956760,
FT ECO:0000269|PubMed:21967437"
FT VARIANT 331
FT /note="I -> M (in strain: Qbeta_2)"
FT /evidence="ECO:0000269|PubMed:19956760"
FT VARIANT 360
FT /note="I -> V (in strain: Qbeta_3_F and Qbeta_3)"
FT /evidence="ECO:0000269|PubMed:19956760,
FT ECO:0000269|PubMed:21967437"
FT VARIANT 374
FT /note="S -> D (in strain: TW18)"
FT /evidence="ECO:0000269|PubMed:19710143"
FT VARIANT 389
FT /note="N -> S (in strain: TW18)"
FT /evidence="ECO:0000269|PubMed:19710143"
FT VARIANT 404
FT /note="F -> Y (in strain: TW18)"
FT /evidence="ECO:0000269|PubMed:19710143"
FT VARIANT 412
FT /note="F -> S (in strain: Qbeta_2_FR and Qbeta_3FR)"
FT /evidence="ECO:0000269|PubMed:19956760,
FT ECO:0000269|PubMed:21967437"
FT VARIANT 418
FT /note="V -> I (in strain: TW18)"
FT /evidence="ECO:0000269|PubMed:19710143"
FT VARIANT 419
FT /note="K -> N (in strain: Qbeta_2_FR)"
FT /evidence="ECO:0000269|PubMed:21967437"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 84..103
FT /evidence="ECO:0007829|PDB:5MNT"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 107..120
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 129..177
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 180..188
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 203..210
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 212..234
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 237..253
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 261..280
FT /evidence="ECO:0007829|PDB:5MNT"
FT TURN 281..286
FT /evidence="ECO:0007829|PDB:5MNT"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 295..303
FT /evidence="ECO:0007829|PDB:5MNT"
FT TURN 304..306
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 317..336
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 341..364
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 367..379
FT /evidence="ECO:0007829|PDB:5MNT"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:5MNT"
FT HELIX 402..416
FT /evidence="ECO:0007829|PDB:5MNT"
SQ SEQUENCE 420 AA; 48547 MW; AF119F7AC04FF950 CRC64;
MPKLPRGLRF GADNEILNDF QELWFPDLFI ESSDTHPWYT LKGRVLNAHL DDRLPNVGGR
QVRRTPHRVT VPIASSGLRP VTTVQYDPAA LSFLLNARVD WDFGNGDSAN LVINDFLFRT
FAPKEFDFSN SLVPRYTQAF SAFNAKYGTM IGEGLETIKY LGLLLRRLRE GYRAVKRGDL
RALRRVIQSY HNGKWKPATA GNLWLEFRYG LMPLFYDIRD VMLDWQNRHD KIQRLLRFSV
GHGEDYVVEF DNLYPAVAYF KLKGEITLER RHRHGISYAN REGYAVFDNG SLRPVSDWKE
LATAFINPHE VAWELTPYSF VVDWFLNVGD ILAQQGQLYH NIDIVDGFDR RDIRLKSFTI
KGERNGRPVN VSASLSAVDL FYSRLHTSNL PFATLDLDTT FSSFKHVLDS IFLLTQRVKR
