ID   SPAN2_BPP21             Reviewed;          62 AA.
AC   P0DOK7;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 1.
DT   23-FEB-2022, entry version 8.
DE   RecName: Full=Spanin, outer lipoprotein subunit {ECO:0000305};
DE            Short=o-spanin {ECO:0000250|UniProtKB:Q37935};
DE   AltName: Full=Lysis protein Rz1 {ECO:0000250|UniProtKB:Q37935};
DE   AltName: Full=Outer membrane lipoprotein Rz1 {ECO:0000250|UniProtKB:Q37935};
DE   Flags: Precursor;
GN   Name=Rz1;
OS   Enterobacteria phage P21 (Bacteriophage 21) (Bacteriophage P21).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Lambdavirus.
OX   NCBI_TaxID=10711;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2019562; DOI=10.1128/jb.173.9.2897-2905.1991;
RA   Bonovich M.T., Young R.;
RT   "Dual start motif in two lambdoid S genes unrelated to lambda S.";
RL   J. Bacteriol. 173:2897-2905(1991).
RN   [2]
RP   FUNCTION.
RX   PubMed=22904283; DOI=10.1128/jb.01245-12;
RA   Berry J., Rajaure M., Pang T., Young R.;
RT   "The spanin complex is essential for lambda lysis.";
RL   J. Bacteriol. 194:5667-5674(2012).
CC   -!- FUNCTION: Component of the spanin complex that disrupts the host outer
CC       membrane and participates in cell lysis during virus exit (Probable).
CC       The spanin complex conducts the final step in host lysis by disrupting
CC       the outer membrane after holin and endolysin action have permeabilized
CC       the inner membrane and degraded the host peptidoglycans (By
CC       similarity). Host outer membrane disruption is due to local fusion
CC       between the inner and outer membrane performed by the spanin complex
CC       (By similarity). {ECO:0000250|UniProtKB:Q37935,
CC       ECO:0000305|PubMed:22904283}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts (via C-terminus) with
CC       the spanin inner membrane subunit (via C-terminus) (By similarity).
CC       Part of the spanin complex which spans the entire periplasmic space.
CC       The spanin complex is composed of one homodimer of the i-spanin linked
CC       by 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 (By similarity).
CC       {ECO:0000250|UniProtKB:Q37935}.
CC   -!- SUBCELLULAR LOCATION: Host cell outer membrane
CC       {ECO:0000250|UniProtKB:Q37935}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:Q37935}; Periplasmic side
CC       {ECO:0000250|UniProtKB:Q37935}.
CC   -!- DOMAIN: The proline-rich region is an essential fusion motif involved
CC       in host membrane fusion leading to lysis.
CC       {ECO:0000250|UniProtKB:Q37935}.
CC   -!- SIMILARITY: Belongs to the Lambdavirus o-spanin family. {ECO:0000305}.
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; M65239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; P0DOK7; -.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0019076; P:viral release from host cell; IEA:InterPro.
DR   InterPro; IPR010346; O-spanin.
DR   Pfam; PF06085; Rz1; 1.
PE   3: Inferred from homology;
KW   Cytolysis; Disulfide bond; Host cell lysis by virus;
KW   Host cell outer membrane; Host membrane; Lipoprotein; Membrane; Palmitate;
KW   Signal; Viral release from host cell.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250|UniProtKB:Q37935"
FT   CHAIN           20..62
FT                   /note="Spanin, outer lipoprotein subunit"
FT                   /id="PRO_0000447229"
FT   TOPO_DOM        20..62
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q37935"
FT   REGION          32..44
FT                   /note="Proline-rich"
FT                   /evidence="ECO:0000250|UniProtKB:Q37935"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q37935"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q37935"
FT   DISULFID        29
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:Q37935"
SQ   SEQUENCE   62 AA;  6955 MW;  6DB9B17AE4E749B8 CRC64;
     MRKLKMMLCV MMLPLVVVGC TSKQSVSQCV KPRLPPAWIM QPPPDFTWQT PLNGIISPSE
     RG