PORTL_BPHA1
ID PORTL_BPHA1 Reviewed; 518 AA.
AC B0ZSF2;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 02-JUN-2021, entry version 27.
DE RecName: Full=Probable portal protein;
GN ORFNames=HAPgp04 {ECO:0000312|EMBL:ABY90372.1};
OS Halomonas phage phiHAP-1 (isolate -/Gulf of Mexico/-/2001) (Bacteriophage
OS phiHAP-1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Hapunavirus.
OX NCBI_TaxID=1283337;
OH NCBI_TaxID=77097; Halomonas aquamarina.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18448537; DOI=10.1128/jvi.00140-08;
RA Mobberley J.M., Authement R.N., Segall A.M., Paul J.H.;
RT "The temperate marine phage PhiHAP-1 of Halomonas aquamarina possesses a
RT linear plasmid-like prophage genome.";
RL J. Virol. 82:6618-6630(2008).
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:0000250|UniProtKB:P03710}.
CC -!- SUBUNIT: Homododecamer. Interacts with the terminase complex composed
CC of two small and one large terminase subunits.
CC {ECO:0000250|UniProtKB:P03710}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03710}.
CC -!- SIMILARITY: Belongs to the siphoviridae portal protein family.
CC {ECO:0000305}.
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; EU399241; ABY90372.1; -; Genomic_DNA.
DR RefSeq; YP_001686740.1; NC_010342.1.
DR GeneID; 5912339; -.
DR KEGG; vg:5912339; -.
DR Proteomes; UP000001179; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0099000; P:viral genome ejection through host cell envelope, contractile tail mechanism; IEA:UniProtKB-KW.
DR GO; GO:0019068; P:virion assembly; IEA:InterPro.
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 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..518
FT /note="Probable portal protein"
FT /id="PRO_0000432541"
FT REGION 492..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..518
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 59388 MW; 18B70B4C38DBAFBE CRC64;
MGLLKRAARA WKLAGQADSP PAQPARKEPT LTRTFKMARQ TRLNNSWTGR SNAGDADHVI
YKDHETLRQR AREQSINSGY AKRFYRLLRQ NVIGPHGITM RSKALKADGY ADDDMRRVIE
QEFKKWSKRG NCDVTGRYSF VTFMWLWIDT LARDGEVMVR ILRNWPNRWG FALQIIESDL
LDTTLNTWLS NGNRVRMGVE IDEWEKPIAY WLKRSHPGDN FERPAEQEYQ RIPADELRLT
FDPWRPHQSR GFTWTHAGAN DLHHVEEYAG AELIAAEQGA KLTGFYEQDA EWVDPPGDED
SDDADQGVII EEIEAGSARL LPYGVTFKPY DNKHPSTNFA PFTKAAVRRI AGAFGPSYNR
LAHDLEGVSF SSLRSGEIDE RDFYKCIQQF AISELLEWVG EVWMECSMLK GVLKIPPRAW
DRLTPIEWLP RGWDWVDPKK DSDAAKTGIE TLTDSVSDIM RRKGRDPDDV YNQISEDIRR
FKRLGIPNPY GKALQANGVT HVEPDEEDDD EPNATGTD