SPAN2_LAMBD
ID SPAN2_LAMBD Reviewed; 60 AA.
AC Q37935;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 99.
DE RecName: Full=Spanin, outer lipoprotein subunit {ECO:0000305};
DE Short=o-spanin {ECO:0000303|PubMed:25870259};
DE AltName: Full=Lysis protein Rz1 {ECO:0000303|PubMed:18713319};
DE AltName: Full=Outer membrane lipoprotein Rz1 {ECO:0000303|PubMed:8626053};
DE Flags: Precursor;
GN Name=Rz1;
OS Escherichia phage lambda (Bacteriophage lambda).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10710;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT "Nucleotide sequence of bacteriophage lambda DNA.";
RL J. Mol. Biol. 162:729-773(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
RX PubMed=8335247; DOI=10.1016/0378-1119(93)90689-z;
RA Hanych B., Kedzierska S., Walderich B., Uznanski B., Taylor A.;
RT "Expression of the Rz gene and the overlapping Rz1 reading frame present at
RT the right end of the bacteriophage lambda genome.";
RL Gene 129:1-8(1993).
RN [3]
RP PROTEIN SEQUENCE OF 20-27, CHARACTERIZATION, DIACYLGLYCEROL AT CYS-20, AND
RP PALMITOYLATION AT CYS-20.
RX PubMed=8626053; DOI=10.1016/0378-1119(95)00712-1;
RA Kedzierska S., Wawrzynow A., Taylor A.;
RT "The Rz1 gene product of bacteriophage lambda is a lipoprotein localized in
RT the outer membrane of Escherichia coli.";
RL Gene 168:1-8(1996).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9158738; DOI=10.1089/mdr.1996.2.147;
RA Taylor A., Kedzierska S., Wawrzynow A.;
RT "Bacteriophage lambda lysis gene product modified and inserted into
RT Escherichia coli outer membrane: Rz1 lipoprotein.";
RL Microb. Drug Resist. 2:147-153(1996).
RN [5]
RP CHARACTERIZATION.
RX PubMed=10651816; DOI=10.1046/j.1432-1327.2000.01051.x;
RA Bryl K., Kedzierska S., Laskowska M., Taylor A.;
RT "Membrane fusion by proline-rich Rz1 lipoprotein, the bacteriophage lambda
RT Rz1 gene product.";
RL Eur. J. Biochem. 267:794-799(2000).
RN [6]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=18713319; DOI=10.1111/j.1365-2958.2008.06408.x;
RA Berry J., Summer E.J., Struck D.K., Young R.;
RT "The final step in the phage infection cycle: the Rz and Rz1 lysis proteins
RT link the inner and outer membranes.";
RL Mol. Microbiol. 70:341-351(2008).
RN [7]
RP SUBUNIT.
RX PubMed=20734329; DOI=10.1002/pro.485;
RA Berry J., Savva C., Holzenburg A., Young R.;
RT "The lambda spanin components Rz and Rz1 undergo tertiary and quaternary
RT rearrangements upon complex formation.";
RL Protein Sci. 19:1967-1977(2010).
RN [8]
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).
RN [9]
RP FUNCTION, SUBUNIT, DISULFIDE BOND, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-29.
RX PubMed=23387988; DOI=10.1111/mmi.12167;
RA Berry J.D., Rajaure M., Young R.;
RT "Spanin function requires subunit homodimerization through intermolecular
RT disulfide bonds.";
RL Mol. Microbiol. 88:35-47(2013).
RN [10]
RP REVIEW.
RX PubMed=24113139; DOI=10.1016/j.mib.2013.08.008;
RA Young R.;
RT "Phage lysis: do we have the hole story yet?";
RL Curr. Opin. Microbiol. 16:790-797(2013).
RN [11]
RP FUNCTION.
RX PubMed=25870259; DOI=10.1073/pnas.1420588112;
RA Rajaure M., Berry J., Kongari R., Cahill J., Young R.;
RT "Membrane fusion during phage lysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:5497-5502(2015).
RN [12]
RP DOMAIN.
RX PubMed=28040784; DOI=10.1534/g3.116.037192;
RA Cahill J., Rajaure M., O'Leary C., Sloan J., Marrufo A., Holt A.,
RA Kulkarni A., Hernandez O., Young R.;
RT "Genetic Analysis of the Lambda Spanins Rz and Rz1: Identification of
RT Functional Domains.";
RL G3 (Bethesda) 7:741-753(2017).
CC -!- FUNCTION: Component of the spanin complex that disrupts the host outer
CC membrane and participates in cell lysis during virus exit
CC (PubMed:22904283, PubMed:23387988, PubMed:25870259). The spanin complex
CC conducts the final step in host lysis by disrupting the outer membrane
CC after holin and endolysin action have permeabilized the inner membrane
CC and degraded the host peptidoglycans (PubMed:25870259). Host outer
CC membrane disruption due to local fusion between the inner and outer
CC membrane performed by the spanin complex (PubMed:25870259).
CC {ECO:0000269|PubMed:22904283, ECO:0000269|PubMed:23387988,
CC ECO:0000269|PubMed:25870259}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (Probable) (PubMed:23387988).
CC Interacts (via C-terminus) with the spanin inner membrane subunit (via
CC C-terminus). Part of the spanin complex which spans the entire
CC periplasmic space (PubMed:23387988). The spanin complex is composed of
CC one homodimer of the i-spanin linked by intermolecular disulfide bonds
CC involving two Cys residues and one homodimer of the o-spanin covalently
CC linked by an intermolecular disulfide bond involving one Cys
CC (PubMed:23387988). {ECO:0000269|PubMed:23387988,
CC ECO:0000305|PubMed:20734329}.
CC -!- SUBCELLULAR LOCATION: Host cell outer membrane
CC {ECO:0000269|PubMed:18713319, ECO:0000269|PubMed:23387988}; Lipid-
CC anchor {ECO:0000269|PubMed:18713319, ECO:0000269|PubMed:23387988};
CC Periplasmic side {ECO:0000269|PubMed:18713319,
CC ECO:0000269|PubMed:23387988}.
CC -!- DOMAIN: The proline-rich region is an essential fusion motif involved
CC in host membrane fusion leading to lysis.
CC {ECO:0000269|PubMed:28040784}.
CC -!- SIMILARITY: Belongs to the Lambdavirus o-spanin family. {ECO:0000305}.
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DR EMBL; J02459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U37314; AAC48862.1; -; Genomic_DNA.
DR PIR; JN0750; JN0750.
DR RefSeq; YP_001551744.1; NC_001416.1.
DR SMR; Q37935; -.
DR IntAct; Q37935; 3.
DR TCDB; 1.M.1.1.1; the rz/rz1 spanin1 (rz(1)) family.
DR GeneID; 5739319; -.
DR KEGG; vg:5739319; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0039662; C:host cell outer membrane; IDA:CACAO.
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:0090680; P:disruption by virus of host outer membrane; IMP:CACAO.
DR GO; GO:0061025; P:membrane fusion; IDA:CACAO.
DR GO; GO:0045861; P:negative regulation of proteolysis; IDA:CACAO.
DR GO; GO:0019076; P:viral release from host cell; IDA:CACAO.
DR InterPro; IPR010346; O-spanin.
DR Pfam; PF06085; Rz1; 1.
PE 1: Evidence at protein level;
KW Cytolysis; Direct protein sequencing; Disulfide bond;
KW Host cell lysis by virus; Host cell outer membrane; Host membrane;
KW Lipoprotein; Membrane; Palmitate; Reference proteome; Signal;
KW Viral release from host cell.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:8626053"
FT CHAIN 20..60
FT /note="Spanin, outer lipoprotein subunit"
FT /id="PRO_0000003363"
FT TOPO_DOM 20..60
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:22904283"
FT REGION 32..44
FT /note="Proline-rich"
FT /evidence="ECO:0000269|PubMed:28040784"
FT LIPID 20
FT /note="N-palmitoyl cysteine; by host"
FT /evidence="ECO:0000269|PubMed:8626053"
FT LIPID 20
FT /note="S-diacylglycerol cysteine; by host"
FT /evidence="ECO:0000269|PubMed:8626053"
FT DISULFID 29
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:23387988"
FT MUTAGEN 29
FT /note="C->S: Complete loss of disulfide-linked homodimers."
FT /evidence="ECO:0000269|PubMed:23387988"
SQ SEQUENCE 60 AA; 6588 MW; 30E5B333E46AB46C CRC64;
MLKLKMMLCV MMLPLVVVGC TSKQSVSQCV KPPPPPAWIM QPPPDWQTPL NGIISPSERG
