ID   SPAN1_BPT4              Reviewed;         117 AA.
AC   P39504;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   23-FEB-2022, entry version 63.
DE   RecName: Full=Spanin, inner membrane subunit;
DE            Short=i-spanin;
GN   Name=y13K; Synonyms=pseT.3;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [2]
RP   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 (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:17900620}.
CC   -!- SUBUNIT: Interacts (via C-terminus) with the spanin outer lipoprotein
CC       subunit (via C-terminus). Part of the spanin complex which spans the
CC       entire periplasmic space. The spanin complex is composed of spanin
CC       inner membrane subunit and spanin outer membrane subunit.
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}; Periplasmic side
CC       {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF158101; AAD42645.1; -; Genomic_DNA.
DR   RefSeq; NP_049837.1; NC_000866.4.
DR   SMR; P39504; -.
DR   TCDB; 1.M.3.1.1; the spanin3 (spanin3) family.
DR   PRIDE; P39504; -.
DR   GeneID; 1258652; -.
DR   KEGG; vg:1258652; -.
DR   Proteomes; UP000009087; 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   GO; GO:0044659; P:viral release from host cell by cytolysis; IGI:CACAO.
PE   3: Inferred from homology;
KW   Coiled coil; Cytolysis; Host cell inner membrane; Host cell lysis by virus;
KW   Host cell membrane; Host membrane; Membrane; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral release from host cell.
FT   CHAIN           1..117
FT                   /note="Spanin, inner membrane subunit"
FT                   /id="PRO_0000165184"
FT   TOPO_DOM        1..2
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3..23
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        24..117
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   COILED          24..93
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   117 AA;  13135 MW;  D8B52577D7DA979B CRC64;
     MHVSNFTAGL LLLVIAFGGT SIILKHKVER LETSVTEITK TANENALALN NLRIQYNYID
     AMNNKNREAI AAIERENEKL RKDAKKADVV AHKPGLVEKQ INNSFNKFAE DIQDLSK