ID   SPAN1_BPKMV             Reviewed;         109 AA.
AC   Q7Y2B9;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   23-FEB-2022, entry version 55.
DE   RecName: Full=Probable spanin, inner membrane subunit;
DE            Short=i-spanin;
GN   ORFNames=46;
OS   Pseudomonas phage phiKMV.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Krylovirinae; Phikmvvirus.
OX   NCBI_TaxID=204270;
OH   NCBI_TaxID=287; Pseudomonas aeruginosa.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12890620; DOI=10.1016/s0042-6822(03)00123-5;
RA   Lavigne R., Burkal'tseva M.V., Robben J., Sykilinda N.N., Kurochkina L.P.,
RA   Grymonprez B., Jonckx B., Krylov V.N., Mesyanzhinov V.V., Volckaert G.;
RT   "The genome of bacteriophage phiKMV, a T7-like virus infecting Pseudomonas
RT   aeruginosa.";
RL   Virology 312:49-59(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15549178; DOI=10.1007/s00018-004-4301-y;
RA   Lavigne R., Briers Y., Hertveldt K., Robben J., Volckaert G.;
RT   "Identification and characterization of a highly thermostable bacteriophage
RT   lysozyme.";
RL   Cell. Mol. Life Sci. 61:2753-2759(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16522177; DOI=10.2174/0929866054696127;
RA   Lavigne R., Roucourt B., Hertveldt K., Volckaert G.;
RT   "Characterization of the bacteriophage PhiKMV DNA ligase.";
RL   Protein Pept. Lett. 12:645-648(2005).
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).
CC       {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}; Periplasmic side
CC       {ECO:0000250}.
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DR   EMBL; AJ505558; CAD44237.1; -; Genomic_DNA.
DR   RefSeq; NP_877485.1; NC_005045.1.
DR   SMR; Q7Y2B9; -.
DR   TCDB; 1.M.1.3.1; the rz/rz1 spanin1 (rz(1)) family.
DR   GeneID; 2641783; -.
DR   KEGG; vg:2641783; -.
DR   Proteomes; UP000000842; 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.
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..109
FT                   /note="Probable spanin, inner membrane subunit"
FT                   /id="PRO_0000429260"
FT   TRANSMEM        1..17
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   COILED          27..63
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   109 AA;  11982 MW;  73DBE47138BFBF4E CRC64;
     MPRTIVAILV LAVVALGASY GFVQSYRALG IAQGEIKRQT ARAEALEVRY ATLQRHVKEV
     AARTNTQRQE VDRALDQNRP WADRPVPAAV VDSLCNRPGA RCAVRTPTD