ID E9KIG6_9CAUD Unreviewed; 519 AA.
AC E9KIG6;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Minor capsid protein {ECO:0000256|HAMAP-Rule:MF_04119};
DE AltName: Full=Minor head protein {ECO:0000256|HAMAP-Rule:MF_04119};
GN ORFNames=phiIBB-PF7Ap27 {ECO:0000313|EMBL:ADV35692.1};
OS Pseudomonas phage phiIBB-PF7A.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Autographiviridae; Studiervirinae; Pifdecavirus; Pifdecavirus IBBPF7A.
OX NCBI_TaxID=942165 {ECO:0000313|EMBL:ADV35692.1, ECO:0000313|Proteomes:UP000007475};
RN [1] {ECO:0000313|EMBL:ADV35692.1, ECO:0000313|Proteomes:UP000007475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21439081;
RA Sillankorva S., Kluskens L.D., Lingohr E.J., Kropinski A.M., Neubauer P.,
RA Azeredo J.;
RT "Complete genome sequence of the lytic Pseudomonas fluorescens phage
RT phiIBB-PF7A.";
RL Virol. J. 8:142-142(2011).
CC -!- FUNCTION: Assembles with the major capsid protein to form an
CC icosahedral capsid. The major and minor capsid proteins are
CC incorporated into the capsid in about a 90/10 ratio respectively. Once
CC the capsid is formed, encapsidates one single copy of the viral genome.
CC {ECO:0000256|HAMAP-Rule:MF_04119}.
CC -!- SUBUNIT: Interacts with the connector protein and the major capsid
CC protein. {ECO:0000256|HAMAP-Rule:MF_04119}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04119}.
CC -!- MISCELLANEOUS: The minor capsid protein is produced by a -1 ribosomal
CC frameshift near the C-terminus of the ORF coding for the major capsid
CC protein, producing a protein with a C-terminal extension compared to
CC the major capsid protein. The major capsid protein is produced by
CC conventional translation of the same ORF. {ECO:0000256|HAMAP-
CC Rule:MF_04119}.
CC -!- SIMILARITY: Belongs to the T7virus minor capsid protein family.
CC {ECO:0000256|HAMAP-Rule:MF_04119}.
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DR EMBL; GU583987; ADV35692.1; -; Genomic_DNA.
DR RefSeq; YP_004306346.1; NC_015264.1.
DR GeneID; 10323814; -.
DR KEGG; vg:10323814; -.
DR OrthoDB; 4979at10239; -.
DR Proteomes; UP000007475; Genome.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.1080; -; 2.
DR HAMAP; MF_04119; CAPSID_PROTEIN_T7; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR049301; Capsid_Gp10A/Gp10B-like_dom.
DR InterPro; IPR039009; Capsid_Gp10A/Gp10B_dom.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR Pfam; PF02368; Big_2; 2.
DR Pfam; PF21703; Gp10A-like; 1.
DR SMART; SM00635; BID_2; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 2.
PE 3: Inferred from homology;
KW Capsid protein {ECO:0000256|HAMAP-Rule:MF_04119};
KW Reference proteome {ECO:0000313|Proteomes:UP000007475};
KW Virion {ECO:0000256|HAMAP-Rule:MF_04119}.
FT DOMAIN 347..423
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
FT DOMAIN 431..511
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
SQ SEQUENCE 519 AA; 54500 MW; A19095AC4B56DE78 CRC64;
MAQMQGGQQI GKDQGKGQNA ADKLALFLKV FGGEVLTAFK RRSVTMDKHM VRTIQSGKSA
QFPVMGRTAG FYLAPGENID DKQGDIKHTE KVITIDGLLV SAVMIFDIED AMNHYDVSSE
YSAQLGEALA ISADGAVLAE MALLCNLPEE SDENIAGLGK ASVLPIGKAA DLMDPEARGK
AILKGLTLAR AKLTKNYVPS SDRFFYTSPE YYSAILAALM PNAANYAALI DPETGNIRNV
MGFTVIEVPH LTVGGSGNDL AGTSRKHAFP QVSSDTVKVA ADNVVGLFNH RSAVGTVKLK
DMALERSRRA NFQGDQIIGK YAMGHGGLRP EAAGALVIEK EGVSVPDPTG VTLSQKTMAL
DVGTSKALTA TVQPVGAPQA VVWQSIDERV AKVSSAGLVE AIGAGTCDIV ATTVNGLSAV
CKVTVKIPNV PVTGVEFSRK DPVELTVGGT YTMTVNVLPA NATNKNVTYE VEDPTIVKLG
GTTGRTVQGL KVGTTVITAT TEDGGFKTEL GFVVKVEAP
//
