SOC_BPT4
ID SOC_BPT4 Reviewed; 80 AA.
AC P03715;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 23-FEB-2022, entry version 83.
DE RecName: Full=Small outer capsid protein {ECO:0000255|HAMAP-Rule:MF_04115};
DE Short=Soc;
GN Name=soc;
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6098451; DOI=10.1002/j.1460-2075.1984.tb02221.x;
RA McDonald P.M., Mosig G.;
RT "Regulation of a new bacteriophage T4 gene, 69, that spans an origin of DNA
RT replication.";
RL EMBO J. 3:2863-2871(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6693022; DOI=10.1093/genetics/106.1.17;
RA Macdonald P.M., Kutter E.M., Mosig G.;
RT "Regulation of a bacteriophage T4 late gene, soc, which maps in an early
RT region.";
RL Genetics 106:17-27(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [4]
RP PROTEIN SEQUENCE OF 2-80.
RX PubMed=642009; DOI=10.1016/0022-2836(78)90066-9;
RA Bijlenga R.K.L., Ishii T., Tsugita A.;
RT "Complete primary structure of the small outer capsid (soc) protein of
RT bacteriophage T4.";
RL J. Mol. Biol. 120:249-263(1978).
RN [5]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH THE MAJOR CAPSID PROTEIN.
RX PubMed=1469720; DOI=10.1016/0022-2836(92)90871-g;
RA Steven A.C., Greenstone H.L., Booy F.P., Black L.W., Ross P.D.;
RT "Conformational changes of a viral capsid protein. Thermodynamic rationale
RT for proteolytic regulation of bacteriophage T4 capsid expansion, co-
RT operativity, and super-stabilization by soc binding.";
RL J. Mol. Biol. 228:870-884(1992).
RN [6]
RP REVIEW.
RX PubMed=21129201; DOI=10.1186/1743-422x-7-356;
RA Rao V.B., Black L.W.;
RT "Structure and assembly of bacteriophage T4 head.";
RL Virol. J. 7:356-356(2010).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS), INTERACTION WITH THE
RP MAJOR CAPSID PROTEIN, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11162794; DOI=10.1006/viro.2000.0735;
RA Olson N.H., Gingery M., Eiserling F.A., Baker T.S.;
RT "The structure of isometric capsids of bacteriophage T4.";
RL Virology 279:385-391(2001).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (22.0 ANGSTROMS), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15071181; DOI=10.1073/pnas.0400444101;
RA Fokine A., Chipman P.R., Leiman P.G., Mesyanzhinov V.V., Rao V.B.,
RA Rossmann M.G.;
RT "Molecular architecture of the prolate head of bacteriophage T4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6003-6008(2004).
CC -!- FUNCTION: Capsid decoration protein which helps to stabilize the capsid
CC against extremes of pH and temperature. Once maturation and expansion
CC of the capsid has occured, trimers of soc attach the interfaces between
CC the hexamer of the major capsid protein. Acts as a 'glue' between
CC neighboring hexameric capsomers. Dispensable for the head morphogenesis
CC and phage infection. {ECO:0000255|HAMAP-Rule:MF_04115,
CC ECO:0000269|PubMed:11162794, ECO:0000269|PubMed:1469720,
CC ECO:0000269|PubMed:15071181}.
CC -!- SUBUNIT: Homotrimer. Interacts with the major capsid protein; three soc
CC molecules associate with each interface between the major capsid
CC protein facets. {ECO:0000255|HAMAP-Rule:MF_04115,
CC ECO:0000269|PubMed:11162794, ECO:0000269|PubMed:1469720}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04115,
CC ECO:0000269|PubMed:11162794, ECO:0000269|PubMed:15071181}. Note=870
CC copies decorate the capsid. {ECO:0000250|UniProtKB:Q7Y5B1}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae Soc family. {ECO:0000255|HAMAP-
CC Rule:MF_04115}.
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DR EMBL; X01416; CAA25663.1; -; Genomic_DNA.
DR EMBL; M30001; AAB07793.1; -; Genomic_DNA.
DR EMBL; K03113; AAA32557.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42659.1; -; Genomic_DNA.
DR PIR; A04342; VHBPC4.
DR RefSeq; NP_049644.1; NC_000866.4.
DR PDB; 5VF3; EM; 3.30 A; O/P/Q/R/S/T/U/V/W/X/Y=1-80.
DR PDBsum; 5VF3; -.
DR SMR; P03715; -.
DR GeneID; 1258783; -.
DR KEGG; vg:1258783; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0098021; C:viral capsid, decoration; IMP:CACAO.
DR Gene3D; 3.90.930.20; -; 1.
DR HAMAP; MF_04115; SOC_T4; 1.
DR InterPro; IPR031743; Soc.
DR InterPro; IPR038151; Soc_sf.
DR Pfam; PF16855; Soc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid decoration protein; Capsid protein;
KW Direct protein sequencing; Reference proteome; Virion.
FT CHAIN 1..80
FT /note="Small outer capsid protein"
FT /id="PRO_0000165074"
FT CONFLICT 40
FT /note="K -> GKEFHK (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="H -> T (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:5VF3"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:5VF3"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:5VF3"
SQ SEQUENCE 80 AA; 9117 MW; E55CAE53A118109C CRC64;
MASTRGYVNI KTFEQKLDGN KKIEGKEISV AFPLYSDVHK ISGAHYQTFP SEKAAYSTVY
EENQRTEWIA ANEDLWKVTG
