ID   SPAN1_BPT7              Reviewed;         143 AA.
AC   P03803;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Spanin, inner membrane subunit {ECO:0000303|PubMed:17900620};
DE            Short=i-spanin;
DE   AltName: Full=Gene product 18.5;
DE            Short=Gp18.5;
GN   OrderedLocusNames=18.5;
OS   Escherichia phage T7 (Bacteriophage T7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX   NCBI_TaxID=10760;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA   Dunn J.J., Studier F.W.;
RT   "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT   T7 genetic elements.";
RL   J. Mol. Biol. 166:477-535(1983).
RN   [2]
RP   INTERACTION WITH O-SPANIN.
RX   PubMed=8528255; DOI=10.1038/ng0196-72;
RA   Bartel P.L., Roecklein J.A., SenGupta D., Fields S.;
RT   "A protein linkage map of Escherichia coli bacteriophage T7.";
RL   Nat. Genet. 12:72-77(1996).
RN   [3]
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=17900620; DOI=10.1016/j.jmb.2007.08.045;
RA   Summer E.J., Berry J., Tran T.A., Niu L., Struck D.K., Young R.;
RT   "Rz/Rz1 lysis gene equivalents in phages of Gram-negative hosts.";
RL   J. Mol. Biol. 373:1098-1112(2007).
CC   -!- FUNCTION: Component of the spanin complex that disrupts the host outer
CC       membrane and participates in cell lysis during virus exit. The spanin
CC       complex conducts the final step in host lysis by disrupting the outer
CC       membrane after holin and endolysin action have permeabilized the inner
CC       membrane and degraded the host peptidoglycans. Host outer membrane
CC       disruption is possibly due to local fusion between the inner and outer
CC       membrane performed by the spanin complex.
CC       {ECO:0000305|PubMed:17900620}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with the spanin outer lipoprotein
CC       subunit (o-spanin) (via C-terminus). Part of the spanin complex which
CC       spans the entire periplasmic space. The spanin complex is composed of
CC       spanin inner membrane subunit and spanin outer membrane subunit.
CC       {ECO:0000305|PubMed:8528255}.
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane
CC       {ECO:0000305|PubMed:17900620}; Single-pass type II membrane protein
CC       {ECO:0000305|PubMed:17900620}; Periplasmic side
CC       {ECO:0000305|PubMed:17900620}.
CC   -!- SIMILARITY: Belongs to the T7likevirus i-spanin family. {ECO:0000305}.
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DR   EMBL; V01146; CAA24438.1; -; Genomic_DNA.
DR   PIR; A04428; Q8BPE7.
DR   RefSeq; NP_042008.1; NC_001604.1.
DR   SMR; P03803; -.
DR   IntAct; P03803; 1.
DR   MINT; P03803; -.
DR   MEROPS; X19.002; -.
DR   GeneID; 1261067; -.
DR   KEGG; vg:1261067; -.
DR   Proteomes; UP000000840; 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:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0019076; P:viral release from host cell; IEA:InterPro.
DR   InterPro; IPR004929; I-spanin.
DR   InterPro; IPR016417; I-spanin_T7likevirus.
DR   Pfam; PF03245; Phage_lysis; 1.
DR   PIRSF; PIRSF004485; T7_18-5_prd; 1.
PE   1: Evidence at protein level;
KW   Cytolysis; Host cell inner membrane; Host cell lysis by virus;
KW   Host cell membrane; Host membrane; Hydrolase; Membrane; Protease;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral release from host cell.
FT   CHAIN           1..143
FT                   /note="Spanin, inner membrane subunit"
FT                   /id="PRO_0000106537"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:17900620"
FT   TRANSMEM        8..24
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..143
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000305|PubMed:17900620"
SQ   SEQUENCE   143 AA;  16243 MW;  7A2634B7C4C16AEE CRC64;
     MLEFLRKLIP WVLAGMLFGL GWHLGSDSMD AKWKQEVHNE YVKRVEAAKS TQRAIDAVSA
     KYQEDLAALE GSTDRIISDL RSDNKRLRVR VKTTGTSDGQ CGFEPDGRAE LDDRDAKRIL
     AVTQKGDAWI RALQDTIREL QRK