G1P_BPI22
ID G1P_BPI22 Reviewed; 365 AA.
AC P15418;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Gene 1 protein;
DE AltName: Full=G1P;
GN Name=I;
OS Enterobacteria phage I2-2 (Bacteriophage I2-2).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Lineavirus.
OX NCBI_TaxID=10869;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1556749; DOI=10.1007/bf00182391;
RA Stassen A.P., Schonmakers E.F., Yu M., Schoenmakers J.G., Konings R.N.H.;
RT "Nucleotide sequence of the genome of the filamentous bacteriophage I2-2:
RT module evolution of the filamentous phage genome.";
RL J. Mol. Evol. 34:141-152(1992).
CC -!- FUNCTION: Isoform G1P plays an essential role in phage assembly. It is
CC required to increase the number of adhesion zones between the inner and
CC outer membranes of the host cell. The extrusion of neo-synthesized
CC phages occurs at these adhesion sites. May be involved with G4P in
CC creating zone through which the phage assembled and extruded (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: Isoform G11P is also involved in phage assembly, probably
CC playing a structural role in the formation of the phage assembly site.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with G4P; this interaction results in a complex that
CC spans the inner an outer host membranes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=G1P; Synonyms=Gene 1 protein;
CC IsoId=P15418-1; Sequence=Displayed;
CC Name=G11P; Synonyms=Gene 11 protein;
CC IsoId=P15418-2; Sequence=VSP_037571;
CC -!- SIMILARITY: Belongs to the inovirus G1P protein family. {ECO:0000305}.
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DR EMBL; X14336; CAA32519.1; -; Genomic_DNA.
DR PIR; S08092; S08092.
DR RefSeq; NP_039622.1; NC_001332.1. [P15418-1]
DR GeneID; 1260724; -.
DR KEGG; vg:1260724; -.
DR Proteomes; UP000000373; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0099045; P:viral extrusion; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR008900; Zot_N.
DR Pfam; PF05707; Zot; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW Alternative initiation; ATP-binding; Host membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral extrusion; Viral release from host cell.
FT CHAIN 1..365
FT /note="Gene 1 protein"
FT /id="PRO_0000098203"
FT TRANSMEM 255..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..241
FT /note="Missing (in isoform G11P)"
FT /evidence="ECO:0000305"
FT /id="VSP_037571"
SQ SEQUENCE 365 AA; 41385 MW; F82FD59CE8C48594 CRC64;
MAVYVVTGKL GAGKTLVAVS RIQRTLAKGG IVATNLNLKL HHFPQVGRYA KQCRVMRIAD
KPTLEDLEAI GRGNLSYDES KNGLIVLDEC GTWFNSRNWS DKSRQPVIDW FLHARKLGWD
VIFIIQDISL MDKQAREALA EHVVYCRRLD KLNIPIIGGL ISVLSGGRLP LPKVHFGIVK
YGDNPQSLTV DKWIYTGTDL YAAYDTKQIF TSDRELSPPF CPVSPYYTHG IFAVKRDAKY
YMRMTKIYFK KMNRVWLMAS FLALGAGVGF FYKSRQINEQ LSNMPVASAQ ANTTKTDHTI
DELPRLSINS FAQMGYDVNV SFKDAKGKIY YSFDLMKSGY ALDIKDSCHI TLRKRNYIQQ
VTCEG
