SPAN1_BPP22
ID SPAN1_BPP22 Reviewed; 145 AA.
AC P13583; Q7PCD4;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 07-APR-2021, entry version 96.
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=Gene product 15;
DE Short=Gp15;
DE AltName: Full=Lysis protein Rz {ECO:0000255|HAMAP-Rule:MF_04137};
GN Name=15;
OS Salmonella phage P22 (Bacteriophage P22).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Lederbergvirus.
OX NCBI_TaxID=10754;
OH NCBI_TaxID=90371; Salmonella typhimurium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2763468; DOI=10.1016/0042-6822(89)90628-4;
RA Casjens S., Eppler K., Parr R., Poteete A.R.;
RT "Nucleotide sequence of the bacteriophage P22 gene 19 to 3 region:
RT identification of a new gene required for lysis.";
RL Virology 171:588-598(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11053393; DOI=10.1128/jb.182.22.6472-6481.2000;
RA Vander Byl C.S., Kropinski A.M.B.;
RT "Sequence of the genome of Salmonella bacteriophage P22.";
RL J. Bacteriol. 182:6472-6481(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12562822; DOI=10.1128/jb.185.4.1475-1477.2003;
RA Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W.,
RA Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A.,
RA Casjens S.R.;
RT "Corrected sequence of the bacteriophage P22 genome.";
RL J. Bacteriol. 185:1475-1477(2003).
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 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 -!- SIMILARITY: Belongs to the Lambdavirus i-spanin family.
CC {ECO:0000255|HAMAP-Rule:MF_04137}.
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DR EMBL; J04356; AAA88341.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75041.2; -; Genomic_DNA.
DR EMBL; BK000583; DAA01041.1; -; Genomic_DNA.
DR PIR; A33080; APBP22.
DR RefSeq; NP_059623.2; NC_002371.2.
DR SMR; P13583; -.
DR MEROPS; X19.001; -.
DR TCDB; 1.M.1.1.4; the rz/rz1 spanin1 (rz(1)) family.
DR GeneID; 1262837; -.
DR KEGG; vg:1262837; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; 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 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..145
FT /note="Spanin, inner membrane subunit"
FT /id="PRO_0000077568"
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..145
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DISULFID 92
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04137"
FT DISULFID 143
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04137"
SQ SEQUENCE 145 AA; 16219 MW; 1ECD8B9BB4CED181 CRC64;
MSRIKAIIAS VIICIIVCLS WAVNHYRDNA ITYKEQRDKA TSIIADMQKR QRDVAELDAR
YTKELADANA TIETLRADVS AGRKRLQVSA TCPKSTTGAS GMGDGESPRL TADAELNYYR
LRSGIDRITA QVNYLQEYIR SQCLK
