SPANU_BPT1
ID SPANU_BPT1 Reviewed; 133 AA.
AC Q6XQ97;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 12-AUG-2020, entry version 43.
DE RecName: Full=U-spanin;
DE AltName: Full=Gene product 11 {ECO:0000305};
DE AltName: Full=Unimolecular spanin {ECO:0000303|PubMed:30135120};
DE AltName: Full=gp11 {ECO:0000303|PubMed:30135120};
DE Flags: Precursor;
GN ORFNames=11;
OS Escherichia phage T1 (Bacteriophage T1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Drexlerviridae; Tunavirinae; Tunavirus.
OX NCBI_TaxID=1921008;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14972552; DOI=10.1016/j.virol.2003.09.020;
RA Roberts M.D., Martin N.L., Kropinski A.M.;
RT "The genome and proteome of coliphage T1.";
RL Virology 318:245-266(2004).
RN [2]
RP FUNCTION, ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP CYS-22 AND 23-SER-THR-24, AND TOPOLOGY.
RX PubMed=30135120; DOI=10.1128/jvi.00380-18;
RA Kongari R., Snowden J., Berry J.D., Young R.;
RT "Localization and Regulation of the T1 Unimolecular Spanin.";
RL J. Virol. 92:0-0(2018).
CC -!- FUNCTION: [Isoform gp11]: Disrupts the host outer membrane and
CC participates in cell lysis during virus exit (PubMed:30135120). The
CC spanin complex conducts the final step in host lysis by disrupting the
CC outer membrane after holin and endolysin action have permeabilized the
CC inner membrane and degraded the host peptidoglycans (PubMed:30135120).
CC Host outer membrane disruption is possibly due to local fusion between
CC the inner and outer membrane performed by the spanin (PubMed:30135120).
CC {ECO:0000269|PubMed:30135120}.
CC -!- FUNCTION: [Isoform gp11a]: Seems to have a dominant negative lysis
CC delay effect on gp11 function. May serve as an intrinsic anti-spanin,
CC providing another level of regulation for u-spanin function.
CC {ECO:0000269|PubMed:30135120}.
CC -!- SUBCELLULAR LOCATION: [Isoform gp11]: Host cell inner membrane; Single-
CC pass membrane protein {ECO:0000269|PubMed:30135120}. Host cell outer
CC membrane; Lipid-anchor {ECO:0000269|PubMed:30135120}. Note=Inserted
CC simultaneously in the host inner membrane and lipid-anchored in the
CC host outer membrane, thereby spaning the whole periplasmic space.
CC {ECO:0000269|PubMed:30135120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=gp11;
CC IsoId=Q6XQ97-1; Sequence=Displayed;
CC Name=gp11a;
CC IsoId=Q6XQ97-2; Sequence=VSP_060154, VSP_060172;
CC Name=gp11a';
CC IsoId=Q6XQ97-3; Sequence=VSP_060155, VSP_060173;
CC -!- MISCELLANEOUS: [Isoform gp11a]: The initiator methionine is coded by a
CC non-canonical GTG valine codon. {ECO:0000269|PubMed:30135120}.
CC -!- MISCELLANEOUS: [Isoform gp11a']: The initiator methionine is coded by a
CC non-canonical GTG valine codon. {ECO:0000269|PubMed:30135120}.
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DR EMBL; AY216660; AAP49988.1; -; Genomic_DNA.
DR RefSeq; YP_003934.1; NC_005833.1. [Q6XQ97-1]
DR SMR; Q6XQ97; -.
DR TCDB; 1.M.2.1.1; the spanin2 (spanin2) family.
DR GeneID; 2773029; -.
DR KEGG; vg:2773029; -.
DR Proteomes; UP000001156; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cytolysis; Host cell inner membrane;
KW Host cell lysis by virus; Host cell membrane; Host cell outer membrane;
KW Host membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Viral release from host cell.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..133
FT /note="U-spanin"
FT /id="PRO_0000429264"
FT TOPO_DOM 22..104
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:30135120"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:30135120"
FT TOPO_DOM 126..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30135120"
FT LIPID 22
FT /note="N-palmitoyl cysteine; by host"
FT /evidence="ECO:0000255"
FT LIPID 22
FT /note="S-diacylglycerol cysteine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..64
FT /note="Missing (in isoform gp11a')"
FT /evidence="ECO:0000269|PubMed:30135120"
FT /id="VSP_060155"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform gp11a)"
FT /evidence="ECO:0000269|PubMed:30135120"
FT /id="VSP_060154"
FT VAR_SEQ 63
FT /note="V -> M (in isoform gp11a)"
FT /evidence="ECO:0000269|PubMed:30135120"
FT /id="VSP_060172"
FT VAR_SEQ 65
FT /note="V -> M (in isoform gp11a')"
FT /evidence="ECO:0000269|PubMed:30135120"
FT /id="VSP_060173"
FT MUTAGEN 22
FT /note="C->S: Complete loss of lysis."
FT /evidence="ECO:0000269|PubMed:30135120"
FT MUTAGEN 23..24
FT /note="ST->DD: Complete loss of lysis."
FT /evidence="ECO:0000269|PubMed:30135120"
SQ SEQUENCE 133 AA; 14176 MW; EC664CEDF5A532C7 CRC64;
MKLKKTCIAI TVAVGVISLS GCSTASALSG LLSDSPDVTA QVGAENTKQL AGVTAKADDK
REVKVSDSNI GKIDSSVKKS VEVSTIQANT VNAESITVTK SGSWYDPVVC WILVFIVLLL
FYFLIRKHEK KEA
