ID   PORTL_BPSAV             Reviewed;         560 AA.
AC   E1XTG6;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   23-FEB-2022, entry version 34.
DE   RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04114};
DE   AltName: Full=gp20 {ECO:0000255|HAMAP-Rule:MF_04114};
GN   ORFNames=Vi01_157c {ECO:0000312|EMBL:CBW38025.1};
OS   Salmonella phage ViI.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Ackermannviridae; Cvivirinae; Kuttervirus.
OX   NCBI_TaxID=1987993 {ECO:0000312|Proteomes:UP000000339};
OH   NCBI_TaxID=90370; Salmonella typhi.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20817773; DOI=10.1128/jb.00659-10;
RA   Pickard D., Toribio A.L., Petty N.K., van Tonder A., Yu L., Goulding D.,
RA   Barrell B., Rance R., Harris D., Wetter M., Wain J., Choudhary J.,
RA   Thomson N., Dougan G.;
RT   "A conserved acetyl esterase domain targets diverse bacteriophages to the
RT   Vi capsular receptor of Salmonella enterica serovar Typhi.";
RL   J. Bacteriol. 192:5746-5754(2010).
CC   -!- FUNCTION: Forms the portal vertex of the capsid. This portal plays
CC       critical roles in head assembly, genome packaging, neck/tail
CC       attachment, and genome ejection. The portal protein multimerizes as a
CC       single ring-shaped homododecamer arranged around a central channel.
CC       Binds to the terminase subunits to form the packaging machine.
CC       {ECO:0000255|HAMAP-Rule:MF_04114}.
CC   -!- SUBUNIT: Homododecamer. Interacts with the large terminase subunit.
CC       Interacts with the major capsid protein. Interacts with the capsid
CC       vertex protein. {ECO:0000255|HAMAP-Rule:MF_04114}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04114}.
CC       Note=Located at a unique 5-fold vertex of the icosahedral capsid.
CC       {ECO:0000255|HAMAP-Rule:MF_04114}.
CC   -!- SIMILARITY: Belongs to the Tevenvirinae portal protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04114, ECO:0000305}.
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DR   EMBL; FQ312032; CBW38025.1; -; Genomic_DNA.
DR   SMR; E1XTG6; -.
DR   Proteomes; UP000000339; Genome.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0099000; P:viral genome ejection through host cell envelope, contractile tail mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0019072; P:viral genome packaging; IEA:UniProtKB-UniRule.
DR   GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04114; PORTAL_T4; 1.
DR   InterPro; IPR010823; Portal_Gp20.
DR   Pfam; PF07230; Portal_Gp20; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Late protein; Reference proteome; Viral capsid assembly;
KW   Viral contractile tail ejection system;
KW   Viral genome ejection through host cell envelope; Viral genome packaging;
KW   Viral penetration into host cytoplasm; Viral release from host cell;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..560
FT                   /note="Portal protein"
FT                   /id="PRO_0000432534"
FT   REGION          526..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   560 AA;  63106 MW;  E21CA18AAC23293B CRC64;
     MAGYGRGFFG LFGGGGLVNA KVDTDKLAQK QDERLLTKAT VVALDDAQDG SIILQGGANT
     YNYVGVESEL LSVKTVVEEY QSMAQQPEIR KAVDIIVNDV VTCEEDETPV TVNLDKVEGI
     SDTVKESITE CFKEVMHLMD FDNTAYQKIR KWYVDGRQAY HVIVDPTNKK GGIKKLVMLD
     SRCIRPVYIV EKAMREGGIE AIESVTLKYY YNPNYNRNQF TGQSGTSQNF QPSQQELVFD
     DESIVYIDSG EEPLANGIVP GLLNPAIRPL NNLVTTEDAT VIYAITRAPE KRAFYLDVGT
     LGKKSAEEYM TMMMGKFKNR NAYDRTTGKI TGNAHLMGIA EDYWLPRREG QNATEIATVG
     GGNQLGEMDH VNYFREKLYD ALMIPKSRLQ EEGSINIGGS NLAEITQEEL RFSKFCAGLR
     RRYSHFFMEF LRRQLILKGV TDEKDWNEKI KPFIKFEFTS DSYIREQQEN AILNDRLASL
     NTVEPFVGSI FSIDYVMRNV LRMSDEEVKE QQAKIAEEKK KGLYPKVQAD ETGNYSGSDV
     SPLKFKPETL PFSGSTDDSI