ID   PORTL_BPN15             Reviewed;         530 AA.
AC   O64319;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   02-DEC-2020, entry version 56.
DE   RecName: Full=Portal protein {ECO:0000255|HAMAP-Rule:MF_04135};
DE   Contains:
DE     RecName: Full=Protein B* {ECO:0000255|HAMAP-Rule:MF_04135};
GN   Name=gene 4 {ECO:0000312|EMBL:AAC19040.1};
OS   Escherichia phage N15 (Bacteriophage N15).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Ravinvirus.
OX   NCBI_TaxID=40631 {ECO:0000312|Proteomes:UP000002132};
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RX   PubMed=10860722; DOI=10.1006/jmbi.2000.3731;
RA   Ravin V., Ravin N., Casjens S., Ford M.E., Hatfull G.F., Hendrix R.W.;
RT   "Genomic sequence and analysis of the atypical temperate bacteriophage
RT   N15.";
RL   J. Mol. Biol. 299:53-73(2000).
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_04135}.
CC   -!- SUBUNIT: Homododecamer. Interacts with the terminase complex composed
CC       of two small and one large terminase subunits. {ECO:0000255|HAMAP-
CC       Rule:MF_04135}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04135}.
CC   -!- PTM: Proteolytically cleaved by the viral protease during capsid
CC       maturation. {ECO:0000255|HAMAP-Rule:MF_04135}.
CC   -!- SIMILARITY: Belongs to the siphoviridae portal protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04135}.
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DR   EMBL; AF064539; AAC19040.1; -; Genomic_DNA.
DR   PIR; T13090; T13090.
DR   RefSeq; NP_046899.1; NC_001901.1.
DR   GeneID; 1261643; -.
DR   KEGG; vg:1261643; -.
DR   Proteomes; UP000002132; Genome.
DR   GO; GO:0046798; C:viral portal complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0099001; P:viral genome ejection through host cell envelope, long flexible tail mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0019068; P:virion assembly; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04135; PORTAL_LAMBDA; 1.
DR   InterPro; IPR006429; Phage_lambda_portal.
DR   Pfam; PF05136; Phage_portal_2; 1.
DR   TIGRFAMs; TIGR01539; portal_lambda; 1.
PE   3: Inferred from homology;
KW   Capsid protein; DNA-binding; Reference proteome; Viral capsid assembly;
KW   Viral genome ejection through host cell envelope; Viral genome packaging;
KW   Viral long flexible tail ejection system;
KW   Viral penetration into host cytoplasm; Viral release from host cell;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..530
FT                   /note="Portal protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04135"
FT                   /id="PRO_0000432542"
FT   CHAIN           20..530
FT                   /note="Protein B*"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04135"
FT                   /id="PRO_0000446428"
FT   SITE            19..20
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04135"
SQ   SEQUENCE   530 AA;  58855 MW;  19FCC4FC57C4C8F2 CRC64;
     MKIPSLVGPD GKTSLREYAG YHGGGGGFGG QLRGWNPPSE SADAALLPNY SRGNARADDL
     VRNNGYAANA VQLHQDHIVG SFFRLSYRPS WRYLGINEED SRAFSRDVEA AWNEYAEDDF
     CGIDAERKRT FTMMIREGVA MHAFNGELCV QATWDSDSTR LFRTQFKMVS PKRVSNPNNI
     GDTRNCRAGV KINDSGAALG YYVSDDGYPG WMAQNWTYIP RELPGGRPSF IHVFEPMEDG
     QTRGANAFYS VMEQMKMLDT LQNTQLQSAI VKAMYAATIE SELDTQSAMD FILGADNKEQ
     QSKLTGWLGE MAAYYSAAPV RLGGARVPHL LPGDSLNLQS AQDTDNGYST FEQSLLRYIA
     AGLGVSYEQL SRNYSQMSYS TARASANESW AYFMGRRKFV ASRQACQMFL CWLEEAIVRR
     VVTLPSKARF SFQEARTAWG NANWIGSGRM AIDGLKEVQE AVMLIEAGLS TYEKECAKRG
     DDYQEIFAQQ VRESMERRAA GLNPPAWAAA AFEAGVKKSN EEEQDGARAA