G1P_BPM13
ID G1P_BPM13 Reviewed; 348 AA.
AC P03656;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Gene 1 protein;
DE AltName: Full=G1P;
GN Name=I;
OS Enterobacteria phage M13 (Bacteriophage M13).
OC Viruses; Monodnaviria; Loebvirae; Hofneiviricota; Faserviricetes;
OC Tubulavirales; Inoviridae; Inovirus.
OX NCBI_TaxID=1977402;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6254849; DOI=10.1016/0378-1119(80)90093-1;
RA van Wezenbeek P.M.G.F., Hulsebos T.J.M., Schoenmakers J.G.G.;
RT "Nucleotide sequence of the filamentous bacteriophage M13 DNA genome:
RT comparison with phage fd.";
RL Gene 11:129-148(1980).
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=P03656-1; Sequence=Displayed;
CC Name=G11P; Synonyms=Gene 11 protein;
CC IsoId=P03656-2; Sequence=VSP_037126;
CC -!- MISCELLANEOUS: [Isoform G11P]: N-formylation on Met-300. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the inovirus G1P protein family. {ECO:0000305}.
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DR EMBL; V00604; CAA23864.1; -; Genomic_DNA.
DR PIR; B04262; Z1BPM3.
DR SMR; P03656; -.
DR Proteomes; UP000002111; 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.
PE 3: Inferred from homology;
KW Alternative initiation; ATP-binding; Formylation; Host membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral extrusion; Viral release from host cell.
FT CHAIN 1..348
FT /note="Gene 1 protein"
FT /id="PRO_0000098206"
FT TRANSMEM 254..270
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..240
FT /note="Missing (in isoform G11P)"
FT /evidence="ECO:0000305"
FT /id="VSP_037126"
SQ SEQUENCE 348 AA; 39551 MW; 355A09850F6D4204 CRC64;
MAVYFVTGKL GSGKTLVSVG KIQDKIVAGC KIATNLDLRL QNLPQVGRFA KTPRVLRIPD
KPSISDLLAI GRGNDSYDEN KNGLLVLDEC GTWFNTRSWN DKERQPIIDW FLHARKLGWD
IIFLVQDLSI VDKQARSALA EHVVYCRRLD RITLPFVGTL YSLITGSKMP LPKLHVGVVK
YGDSQLSPTV ERWLYTGKNL YNAYDTKQAF SSNYDSGVYS YLTPYLSHGR YFKPLNLGQK
MKLTKIYLKK FSRVLCLAIG FASAFTYSYI TQPKPEVKKV VSQTYDFDKF TIDSSQRLNL
SYRYVFKDSK GKLINSDDLQ KQGYSLTYID LCTVSIKKGN SNEIVKCN