SPAN1_LAMBD
ID SPAN1_LAMBD Reviewed; 153 AA.
AC P00726;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 07-APR-2021, entry version 91.
DE RecName: Full=Spanin, inner membrane subunit {ECO:0000255|HAMAP-Rule:MF_04137};
DE Short=i-spanin {ECO:0000255|HAMAP-Rule:MF_04137, ECO:0000303|PubMed:25870259};
DE AltName: Full=Lysis protein Rz {ECO:0000255|HAMAP-Rule:MF_04137, ECO:0000303|PubMed:18713319};
GN Name=Rz;
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 [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 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 [3]
RP INTERACTION WITH SPANIN OUTER LIPOPROTEIN 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 [4]
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 [5]
RP FUNCTION, SUBUNIT, DISULFIDE BOND, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-99 AND CYS-152.
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 [6]
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 [7]
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 [8]
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 have permeabilized the inner membrane and
CC degraded the host peptidoglycans (PubMed:25870259). Host outer membrane
CC disruption is due to local fusion between the inner and outer membrane
CC performed by the spanin complex (PubMed:25870259). {ECO:0000255|HAMAP-
CC Rule:MF_04137, ECO:0000269|PubMed:22904283,
CC ECO:0000269|PubMed:23387988, ECO:0000269|PubMed:25870259}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:23387988). Interacts (via
CC C-terminus) with the spanin outer lipoprotein subunit (via C-terminus)
CC (PubMed:20734329). 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:0000255|HAMAP-Rule:MF_04137,
CC ECO:0000269|PubMed:20734329, ECO:0000269|PubMed:23387988}.
CC -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_04137, ECO:0000269|PubMed:18713319}; Single-pass type II
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04137,
CC ECO:0000269|PubMed:18713319}; Periplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_04137, ECO:0000269|PubMed:18713319}.
CC -!- DOMAIN: The coiled coil region is probably involved in host membrane
CC fusion leading to lysis. {ECO:0000255|HAMAP-Rule:MF_04137,
CC ECO:0000269|PubMed:28040784}.
CC -!- SIMILARITY: Belongs to the Lambdavirus i-spanin family.
CC {ECO:0000255|HAMAP-Rule:MF_04137}.
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DR EMBL; J02459; AAA96599.1; -; Genomic_DNA.
DR PIR; A94614; APBPML.
DR RefSeq; NP_040646.1; NC_001416.1.
DR SMR; P00726; -.
DR MEROPS; X19.001; -.
DR TCDB; 1.M.1.1.1; the rz/rz1 spanin1 (rz(1)) family.
DR PRIDE; P00726; -.
DR GeneID; 2703481; -.
DR KEGG; vg:2703481; -.
DR Proteomes; UP000001711; 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:0090680; P:disruption by virus of host outer membrane; IMP:CACAO.
DR GO; GO:0061025; P:membrane fusion; IDA:CACAO.
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 1: Evidence at protein level;
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..153
FT /note="Spanin, inner membrane subunit"
FT /id="PRO_0000077571"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:18713319"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..153
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:18713319"
FT COILED 65..92
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04137"
FT DISULFID 99
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04137,
FT ECO:0000269|PubMed:23387988"
FT DISULFID 152
FT /note="Interchain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04137,
FT ECO:0000269|PubMed:23387988"
FT MUTAGEN 99
FT /note="C->S: Complete loss of disulfide-linked homodimers;
FT when associated with S-152."
FT /evidence="ECO:0000269|PubMed:23387988"
FT MUTAGEN 152
FT /note="C->S: Complete loss of disulfide-linked homodimers;
FT when associated with S-99."
FT /evidence="ECO:0000269|PubMed:23387988"
SQ SEQUENCE 153 AA; 17230 MW; E661C54AA289230A CRC64;
MSRVTAIISA LVICIIVCLS WAVNHYRDNA ITYKAQRDKN ARELKLANAA ITDMQMRQRD
VAALDAKYTK ELADAKAEND ALRDDVAAGR RRLHIKAVCQ SVREATTASG VDNAASPRLA
DTAERDYFTL RERLITMQKQ LEGTQKYINE QCR
