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CAPSB_BPT7
ID   CAPSB_BPT7              Reviewed;         398 AA.
AC   P19727; P03717;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   23-FEB-2022, entry version 70.
DE   RecName: Full=Minor capsid protein {ECO:0000255|HAMAP-Rule:MF_04119};
DE   AltName: Full=Gene product 10B;
DE            Short=Gp10B;
DE   AltName: Full=Minor head protein {ECO:0000255|HAMAP-Rule:MF_04119};
GN   OrderedLocusNames=10;
OS   Escherichia phage T7 (Bacteriophage T7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX   NCBI_TaxID=10760;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA   Dunn J.J., Studier F.W.;
RT   "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT   T7 genetic elements.";
RL   J. Mol. Biol. 166:477-535(1983).
RN   [2]
RP   RIBOSOMAL FRAMESHIFT.
RX   PubMed=1938901; DOI=10.1128/jb.173.21.6998-7003.1991;
RA   Condron B.G., Atkins J.F., Gesteland R.F.;
RT   "Frameshifting in gene 10 of bacteriophage T7.";
RL   J. Bacteriol. 173:6998-7003(1991).
RN   [3]
RP   INTERACTION WITH THE MAJOR CAPSID PROTEIN, FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=20962334; DOI=10.1074/jbc.m110.187211;
RA   Ionel A., Velazquez-Muriel J.A., Luque D., Cuervo A., Caston J.R.,
RA   Valpuesta J.M., Martin-Benito J., Carrascosa J.L.;
RT   "Molecular rearrangements involved in the capsid shell maturation of
RT   bacteriophage T7.";
RL   J. Biol. Chem. 286:234-242(2011).
RN   [4]
RP   INTERACTION WITH THE CONNECTOR PROTEIN.
RX   PubMed=23580619; DOI=10.1073/pnas.1215563110;
RA   Guo F., Liu Z., Vago F., Ren Y., Wu W., Wright E.T., Serwer P., Jiang W.;
RT   "Visualization of uncorrelated, tandem symmetry mismatches in the internal
RT   genome packaging apparatus of bacteriophage T7.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6811-6816(2013).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=23884409; DOI=10.1074/jbc.m113.491209;
RA   Cuervo A., Pulido-Cid M., Chagoyen M., Arranz R., Gonzalez-Garcia V.A.,
RA   Garcia-Doval C., Caston J.R., Valpuesta J.M., van Raaij M.J.,
RA   Martin-Benito J., Carrascosa J.L.;
RT   "Structural characterization of the bacteriophage T7 tail machinery.";
RL   J. Biol. Chem. 288:26290-26299(2013).
CC   -!- FUNCTION: Assembles with the major capsid protein to form an
CC       icosahedral capsid with a T=7 symmetry, about 60 nm in diameter, and
CC       consisting of 415 capsid proteins (PubMed:20962334). The major and
CC       minor capsid proteins are incorporated into the capsid in about a 90/10
CC       ratio respectively. Once the capsid formed, encapsidates one single
CC       copy of the viral genome. {ECO:0000269|PubMed:20962334}.
CC   -!- SUBUNIT: Interacts with the connector protein and the major capsid
CC       protein. {ECO:0000255|HAMAP-Rule:MF_04119, ECO:0000269|PubMed:20962334,
CC       ECO:0000269|PubMed:23580619}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04119,
CC       ECO:0000269|PubMed:20962334, ECO:0000269|PubMed:23884409}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Ribosomal frameshifting; Named isoforms=2;
CC       Name=VC10B; Synonyms=Minor capsid protein 10B;
CC         IsoId=P19727-1; Sequence=Displayed;
CC       Name=VC10A; Synonyms=Major capsid protein 10A;
CC         IsoId=P19726-1; Sequence=External;
CC   -!- MISCELLANEOUS: The minor capsid protein is produced by a -1 ribosomal
CC       frameshift near the C-terminus of the ORF coding for the major capsid
CC       protein, producing a protein with a C-terminal extension compared to
CC       the major capsid protein. The major capsid protein is produced by
CC       conventional translation of the same ORF. {ECO:0000255|HAMAP-
CC       Rule:MF_04119}.
CC   -!- MISCELLANEOUS: [Isoform VC10B]: Produced by -1 ribosomal frameshifting.
CC       {ECO:0000269|PubMed:1938901}.
CC   -!- SIMILARITY: Belongs to the T7virus minor capsid protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04119}.
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DR   EMBL; V01146; CAA24428.1; -; Genomic_DNA.
DR   PIR; B04344; VBBPA7.
DR   RefSeq; NP_041997.1; NC_001604.1. [P19727-1]
DR   SMR; P19727; -.
DR   GeneID; 1261029; -.
DR   KEGG; vg:1261029; -.
DR   Proteomes; UP000000840; Genome.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04119; CAPSID_PROTEIN_T7; 1.
DR   InterPro; IPR039009; Capsid_Gp10A/Gp10B.
PE   1: Evidence at protein level;
KW   Capsid protein; Reference proteome; Ribosomal frameshifting; Virion.
FT   CHAIN           1..398
FT                   /note="Minor capsid protein"
FT                   /id="PRO_0000106523"
FT   REGION          359..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   398 AA;  41830 MW;  97919FE8D4FE317A CRC64;
     MASMTGGQQM GTNQGKGVVA AGDKLALFLK VFGGEVLTAF ARTSVTTSRH MVRSISSGKS
     AQFPVLGRTQ AAYLAPGENL DDKRKDIKHT EKVITIDGLL TADVLIYDIE DAMNHYDVRS
     EYTSQLGESL AMAADGAVLA EIAGLCNVES KYNENIEGLG TATVIETTQN KAALTDQVAL
     GKEIIAALTK ARAALTKNYV PAADRVFYCD PDSYSAILAA LMPNAANYAA LIDPEKGSIR
     NVMGFEVVEV PHLTAGGAGT AREGTTGQKH VFPANKGEGN VKVAKDNVIG LFMHRSAVGT
     VKLRDLALER ARRANFQADQ IIAKYAMGHG GLRPEAAGAV VFQSGVMLGV ASTVAASPEE
     ASVTSTEETL TPAQEAARTR AANKARKEAE LAAATAEQ
 
 
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