ID   SOC_BPR69               Reviewed;          78 AA.
AC   Q7Y5B1;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   02-JUN-2021, entry version 60.
DE   RecName: Full=Small outer capsid protein {ECO:0000255|HAMAP-Rule:MF_04115};
DE            Short=Soc;
OS   Escherichia phage RB69 (Bacteriophage RB69).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Mosigvirus.
OX   NCBI_TaxID=12353;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11114936; DOI=10.1128/jb.183.1.358-366.2001;
RA   Tetart F., Desplats C., Kutateladze M., Monod C., Ackermann H.W.,
RA   Krisch H.M.;
RT   "Phylogeny of the major head and tail genes of the wide-ranging T4-type
RT   bacteriophages.";
RL   J. Bacteriol. 183:358-366(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Petrov V., Nolan J., Chin D., Letarov A., Krisch H.M., Karam J.D.;
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0007744|PDB:3IG9, ECO:0007744|PDB:3IGE}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBCELLULAR LOCATION.
RX   PubMed=19835886; DOI=10.1016/j.jmb.2009.10.007;
RA   Qin L., Fokine A., O'Donnell E., Rao V.B., Rossmann M.G.;
RT   "Structure of the small outer capsid protein, Soc: a clamp for stabilizing
RT   capsids of T4-like phages.";
RL   J. Mol. Biol. 395:728-741(2010).
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   -!- 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   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04115,
CC       ECO:0000269|PubMed:19835886}. Note=870 copies decorate the capsid.
CC       {ECO:0000269|PubMed:19835886}.
CC   -!- SIMILARITY: Belongs to the Tevenvirinae Soc family. {ECO:0000255|HAMAP-
CC       Rule:MF_04115}.
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DR   EMBL; AY303349; AAP75929.1; -; Genomic_DNA.
DR   RefSeq; NP_861717.1; NC_004928.1.
DR   PDB; 3IG9; X-ray; 1.90 A; A/B/C/D=1-78.
DR   PDB; 3IGE; X-ray; 2.25 A; A/B=1-78.
DR   PDBsum; 3IG9; -.
DR   PDBsum; 3IGE; -.
DR   SMR; Q7Y5B1; -.
DR   GeneID; 1494143; -.
DR   KEGG; vg:1494143; -.
DR   EvolutionaryTrace; Q7Y5B1; -.
DR   Proteomes; UP000000876; Genome.
DR   GO; GO:0098021; C:viral capsid, decoration; IEA:UniProtKB-UniRule.
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   Reference proteome; Virion.
FT   CHAIN           1..78
FT                   /note="Small outer capsid protein"
FT                   /id="PRO_0000442455"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:3IG9"
FT   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:3IG9"
FT   STRAND          24..28
FT                   /evidence="ECO:0007829|PDB:3IG9"
FT   HELIX           29..34
FT                   /evidence="ECO:0007829|PDB:3IG9"
FT   STRAND          43..50
FT                   /evidence="ECO:0007829|PDB:3IG9"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:3IG9"
FT   HELIX           60..68
FT                   /evidence="ECO:0007829|PDB:3IG9"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:3IG9"
SQ   SEQUENCE   78 AA;  8554 MW;  95A409AC4455FEB1 CRC64;
     MGGYVNIKTF THPAGEGKEV KGMEVSVPFE IYSNEHRIAD AHYQTFPSEK AAYTTVVTDA
     ADWRTKNAAM FTPTPVSG