ID A0A6B9XXA0_9CAUD Unreviewed; 525 AA. AC A0A6B9XXA0; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 07-OCT-2020, entry version 3. DE RecName: Full=Portal protein {ECO:0000256|HAMAP-Rule:MF_04114}; DE AltName: Full=gp20 {ECO:0000256|HAMAP-Rule:MF_04114}; GN ORFNames=CPT_CIP9_291 {ECO:0000313|EMBL:QHS01827.1}; OS Enterobacter phage vB_EclM_CIP9. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Caudovirales; Myoviridae; Tevenvirinae; unclassified Tevenvirinae. OX NCBI_TaxID=2696340 {ECO:0000313|EMBL:QHS01827.1, ECO:0000313|Proteomes:UP000465071}; RN [1] {ECO:0000313|Proteomes:UP000465071} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wang K., Tamayo M.G., Penner T.V., Cook B.W.M., Court D.A., Theriault S.S.; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. 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:0000256|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:0000256|HAMAP-Rule:MF_04114}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04114}. CC Note=Located at a unique 5-fold vertex of the icosahedral capsid. CC {ECO:0000256|HAMAP-Rule:MF_04114}. CC -!- SIMILARITY: Belongs to the Tevenvirinae portal protein family. CC {ECO:0000256|HAMAP-Rule:MF_04114}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MN882610; QHS01827.1; -; Genomic_DNA. DR Proteomes; UP000465071; 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; Peptidase_S80; 1. PE 3: Inferred from homology; KW Capsid protein {ECO:0000256|HAMAP-Rule:MF_04114}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Reference proteome {ECO:0000313|Proteomes:UP000465071}; KW Viral capsid assembly {ECO:0000256|HAMAP-Rule:MF_04114}; KW Viral contractile tail ejection system {ECO:0000256|HAMAP-Rule:MF_04114}; KW Viral genome ejection through host cell envelope {ECO:0000256|HAMAP- KW Rule:MF_04114}; Viral genome packaging {ECO:0000256|HAMAP-Rule:MF_04114}; KW Viral penetration into host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04114}; KW Viral release from host cell {ECO:0000256|HAMAP-Rule:MF_04114}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04114}; KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04114}. FT COILED 70..90 FT /evidence="ECO:0000256|SAM:Coils" SQ SEQUENCE 525 AA; 61023 MW; 311C2CBBBF4C2331 CRC64; MAGFNNGILS IFAPWAKADE NEYKEQINND LESITAPKFD DGAREIETNE REVPYNALMQ QMFGNNEPTL KNTRELIDTY RNLMNNYEVD NAVANIVSDA IVYEDDHDVV ALNLDGTDFS QNIKDRILDE FSEVLNCLHF QRKGIDHFQR WYVDSRIFFH KIVDPKNLKA GIQELRRLDP RQMQFVREVI TKDEAGVKIV KGYKEYFIYD TGHESYACDG RIYEAGTKIK IPRSAIVYAH SGLLSCCGKN IIGYLHRAIK PANQLKLMED ALVIYRITRA PDRRVFYIDT GNMPSRKAAA HMQHIMNTMK NRVVYDATTG KIKNQQHNMS MTEDYWLQRR DGKAVTEVDT MPGASGMSDM DDVRYFRQSL YRALHIPESR IPSDQNSGVM FDAGATISRD ELAFAKWIRQ LQNKFEEIFL DPLKTNLILK KVITEDEWDK EINNVKVVFN RDSYFTEMKD AEIMERRINM LTMAEPFVGK YISHQTAMKD FLQMSDEQIN QEAKQIELES TEARFQNPDE EEEEF //