ID   SPAN1_BP933             Reviewed;         154 AA.
AC   Q9XJJ6;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   02-DEC-2020, entry version 58.
DE   RecName: Full=Spanin, inner membrane subunit {ECO:0000255|HAMAP-Rule:MF_04137};
DE            Short=i-spanin {ECO:0000255|HAMAP-Rule:MF_04137};
DE   AltName: Full=Lysis protein Rz {ECO:0000255|HAMAP-Rule:MF_04137};
GN   Name=Rz;
OS   Escherichia phage 933W (Bacteriophage 933W).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Podoviridae; Sepvirinae; Traversvirus.
OX   NCBI_TaxID=10730;
OH   NCBI_TaxID=83334; Escherichia coli O157:H7.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10074068; DOI=10.1128/jb.181.6.1767-1778.1999;
RA   Plunkett G. III, Rose D.J., Durfee T.J., Blattner F.R.;
RT   "Sequence of Shiga toxin 2 phage 933W from Escherichia coli O157:H7: Shiga
RT   toxin as a phage late-gene product.";
RL   J. Bacteriol. 181:1767-1778(1999).
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 have permeabilized the inner
CC       membrane and degraded the host peptidoglycans. Host outer membrane
CC       disruption is due to local fusion between the inner and outer membrane
CC       performed by the spanin complex. {ECO:0000255|HAMAP-Rule:MF_04137}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts (via C-terminus) with
CC       the spanin outer lipoprotein subunit (via C-terminus). Part of the
CC       spanin complex which spans the entire periplasmic space. The spanin
CC       complex is composed of one homodimer of the i-spanin linked by
CC       intermolecular disulfide bonds involving two Cys residues and one
CC       homodimer of the o-spanin covalently linked by an intermolecular
CC       disulfide bond involving one Cys. {ECO:0000255|HAMAP-Rule:MF_04137}.
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04137}; Single-pass type II membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04137}; Periplasmic side {ECO:0000255|HAMAP-
CC       Rule:MF_04137}.
CC   -!- DOMAIN: The coiled coil region is probably involved in host membrane
CC       fusion leading to lysis. {ECO:0000255|HAMAP-Rule:MF_04137}.
CC   -!- SIMILARITY: Belongs to the Lambdavirus i-spanin family.
CC       {ECO:0000255|HAMAP-Rule:MF_04137}.
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DR   EMBL; AF125520; AAD25452.1; -; Genomic_DNA.
DR   RefSeq; NP_049507.1; NC_000924.1.
DR   SMR; Q9XJJ6; -.
DR   GeneID; 1262012; -.
DR   KEGG; vg:1262012; -.
DR   Proteomes; UP000002135; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0044659; P:viral release from host cell by cytolysis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04137; I_SPANIN_LAMBDA; 1.
DR   InterPro; IPR004929; I-spanin.
DR   Pfam; PF03245; Phage_lysis; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Cytolysis; Disulfide bond; Host cell inner membrane;
KW   Host cell lysis by virus; Host cell membrane; Host membrane; Membrane;
KW   Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW   Viral release from host cell.
FT   CHAIN           1..154
FT                   /note="Spanin, inner membrane subunit"
FT                   /id="PRO_0000423377"
FT   TOPO_DOM        1..3
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        4..24
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        25..154
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   COILED          37..92
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04137"
FT   DISULFID        99
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04137"
FT   DISULFID        153
FT                   /note="Interchain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04137"
SQ   SEQUENCE   154 AA;  17320 MW;  10F58A55841EA027 CRC64;
     MNRVLCVVII VLAVGYGALW LATNHYRDNA LTYKAQRDKK ARELEQANAT ITDMQVRQRD
     VAALDAKYSR ELADARAENE TLRADVAAGR KRLRINATCS GTVREATGTS GVDNATGPRL
     ADTAERDYFI LRERLITMQK QLEGTQKYIN EQCR