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Antiholin (Lysis inhibitor S-107)

 HOLIN_LAMBD             Reviewed;         107 AA.
P03705;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
05-JUL-2017, entry version 103.
RecName: Full=Antiholin {ECO:0000303|PubMed:8878031};
AltName: Full=Lysis inhibitor S-107 {ECO:0000303|PubMed:8878031};
Name=S;
Escherichia phage lambda (Bacteriophage lambda).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Siphoviridae;
Lambdavirus.
NCBI_TaxID=10710;
NCBI_TaxID=562; Escherichia coli.
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
"Nucleotide sequence of bacteriophage lambda DNA.";
J. Mol. Biol. 162:729-773(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS.
PubMed=2943725; DOI=10.1128/jb.167.3.1035-1042.1986;
Raab R., Neal G., Garrett J., Grimaila R., Fusselman R., Young R.;
"Mutational analysis of bacteriophage lambda lysis gene S.";
J. Bacteriol. 167:1035-1042(1986).
[3]
FUNCTION, AND ALTERNATIVE INITIATION.
PubMed=8878031; DOI=10.1046/j.1365-2958.1996.331395.x;
Blasi U., Young R.;
"Two beginnings for a single purpose: the dual-start holins in the
regulation of phage lysis.";
Mol. Microbiol. 21:675-682(1996).
[4]
TOPOLOGY.
PubMed=10217787;
Blasi U., Fraisl P., Chang C.Y., Zhang N., Young R.;
"The C-terminal sequence of the lambda holin constitutes a cytoplasmic
regulatory domain.";
J. Bacteriol. 181:2922-2929(1999).
[5]
FUNCTION (ISOFORM ANTIHOLIN), AND ALTERNATIVE INITIATION.
PubMed=2138979;
Blasi U., Chang C.Y., Zagotta M.T., Nam K.B., Young R.;
"The lethal lambda S gene encodes its own inhibitor.";
EMBO J. 9:981-989(1990).
[6]
SUBCELLULAR LOCATION.
PubMed=2137120;
Zagotta M.T., Wilson D.B.;
"Oligomerization of the bacteriophage lambda S protein in the inner
membrane of Escherichia coli.";
J. Bacteriol. 172:912-921(1990).
[7]
INTERACTION OF ISOFORM HOLIN WITH ISOFORM ANTIHOLIN.
PubMed=11029427; DOI=10.1128/JB.182.21.6075-6081.2000;
Grundling A., Smith D.L., Blasi U., Young R.;
"Dimerization between the holin and holin inhibitor of phage lambda.";
J. Bacteriol. 182:6075-6081(2000).
[8]
SUBUNIT, AND MUTAGENESIS OF ALA-48; CYS-51 AND ALA-52.
PubMed=11029428; DOI=10.1128/JB.182.21.6082-6090.2000;
Grundling A., Blasi U., Young R.;
"Genetic and biochemical analysis of dimer and oligomer interactions
of the lambda S holin.";
J. Bacteriol. 182:6082-6090(2000).
[9]
FUNCTION OF ISOFORM HOLIN.
PubMed=18573181; DOI=10.1111/j.1365-2958.2008.06335.x;
Krupovic M., Bamford D.H.;
"Holin of bacteriophage lambda: structural insights into a membrane
lesion.";
Mol. Microbiol. 69:781-783(2008).
[10]
FUNCTION OF ISOFORM HOLIN.
PubMed=18788120; DOI=10.1111/j.1365-2958.2008.06298.x;
Savva C.G., Dewey J.S., Deaton J., White R.L., Struck D.K.,
Holzenburg A., Young R.;
"The holin of bacteriophage lambda forms rings with large diameter.";
Mol. Microbiol. 69:784-793(2008).
[11]
TOPOLOGY, AND FORMYLATION AT MET-1 (ISOFORM HOLIN).
PubMed=19897658; DOI=10.1128/JB.01263-09;
White R., Tran T.A., Dankenbring C.A., Deaton J., Young R.;
"The N-terminal transmembrane domain of lambda S is required for holin
but not antiholin function.";
J. Bacteriol. 192:725-733(2010).
[12]
FUNCTION.
PubMed=21187415; DOI=10.1073/pnas.1011921108;
White R., Chiba S., Pang T., Dewey J.S., Savva C.G., Holzenburg A.,
Pogliano K., Young R.;
"Holin triggering in real time.";
Proc. Natl. Acad. Sci. U.S.A. 108:798-803(2011).
[13]
REVIEW.
PubMed=24113139; DOI=10.1016/j.mib.2013.08.008;
Young R.;
"Phage lysis: do we have the hole story yet?";
Curr. Opin. Microbiol. 16:790-797(2013).
-!- FUNCTION: Isoform Holin: Accumulates harmlessly in the cytoplasmic
membrane until it reaches a critical concentration that triggers
the formation of micron-scale pores (holes) causing host cell
membrane disruption and endolysin escape into the periplasmic
space. Determines the precise timing of host cell lysis.
Participates with the endolysin and spanin proteins in the
sequential events which lead to the programmed host cell lysis
releasing the mature viral particles from the host cell.
{ECO:0000269|PubMed:18573181, ECO:0000269|PubMed:18788120}.
-!- FUNCTION: Isoform Antiholin: Counteracts the aggregation of the
holin molecules and thus of pore formation.
{ECO:0000269|PubMed:2138979}.
-!- SUBUNIT: Homomultimer (PubMed:11029428). Isoform Holin interacts
with isoform Antiholin; this interaction blocks the holin
homomultimerization and delays host cell lysis (PubMed:11029427).
{ECO:0000269|PubMed:11029427, ECO:0000269|PubMed:11029428}.
-!- SUBCELLULAR LOCATION: Host cell inner membrane
{ECO:0000269|PubMed:2137120}; Multi-pass membrane protein
{ECO:0000269|PubMed:19897658}. Note=Classified as a class I holin.
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Antiholin; Synonyms=Lysis inhibitor S-107
{ECO:0000303|PubMed:2138979, ECO:0000303|PubMed:8878031};
IsoId=P03705-1; Sequence=Displayed;
Name=Holin {ECO:0000303|PubMed:8878031}; Synonyms=Lysis protein
S-105 {ECO:0000303|PubMed:2138979, ECO:0000303|PubMed:8878031};
IsoId=P03705-2; Sequence=VSP_018685;
Note=Contains a N-formylmethionine at position 1.
{ECO:0000269|PubMed:19897658};
-!- INDUCTION: Expressed in the late phase of the viral replicative
cycle.
-!- DOMAIN: Isoform Holin: Has 3 transmembrane regions whereas isoform
Antiholin lacks the first transmembrane region.
{ECO:0000269|PubMed:19897658}.
-!- DOMAIN: The C-terminus acts as a cytoplasmic regulatory region.
-!- SIMILARITY: Belongs to the lambdalikevirus holin family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J02459; AAA96597.1; -; Genomic_DNA.
EMBL; M14035; AAA32248.1; -; Genomic_DNA.
PIR; H94164; YVBPL.
RefSeq; NP_040644.1; NC_001416.1. [P03705-1]
RefSeq; YP_001551775.1; NC_001416.1. [P03705-2]
IntAct; P03705; 3.
TCDB; 1.E.2.1.1; the holin s (holin) family.
GeneID; 2703479; -.
GeneID; 5740919; -.
KEGG; vg:2703479; -.
KEGG; vg:5740919; -.
OrthoDB; VOG090001HJ; -.
Proteomes; UP000001711; Genome.
GO; GO:0020002; C:host cell plasma membrane; IDA:CACAO.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0034291; F:canonical holin activity; IMP:CACAO.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0044659; P:cytolysis by virus of host cell; IDA:UniProtKB.
InterPro; IPR006481; Phage_lambda_GpS_holin.
Pfam; PF05106; Phage_holin_3_1; 1.
TIGRFAMs; TIGR01594; holin_lambda; 1.
1: Evidence at protein level;
Alternative initiation; Complete proteome; Cytolysis; Formylation;
Host cell inner membrane; Host cell lysis by virus;
Host cell membrane; Host membrane; Late protein; Membrane;
Reference proteome; Transmembrane; Transmembrane helix;
Virus exit from host cell.
CHAIN 1 107 Antiholin.
/FTId=PRO_0000003370.
TOPO_DOM 1 37 Cytoplasmic; in isoform Antiholin.
{ECO:0000269|PubMed:19897658}.
TOPO_DOM 1 8 Periplasmic; in isoform Holin.
{ECO:0000269|PubMed:19897658}.
TRANSMEM 9 28 Helical; Note=In isoform Holin.
{ECO:0000255}.
TOPO_DOM 29 37 Cytoplasmic; in isoform Holin.
{ECO:0000269|PubMed:19897658}.
TRANSMEM 38 58 Helical. {ECO:0000255}.
TOPO_DOM 59 70 Periplasmic.
{ECO:0000269|PubMed:19897658}.
TRANSMEM 71 91 Helical. {ECO:0000255}.
TOPO_DOM 92 107 Cytoplasmic.
{ECO:0000305|PubMed:10217787}.
VAR_SEQ 1 2 Missing (in isoform Holin).
{ECO:0000269|PubMed:2138979,
ECO:0000269|PubMed:8878031}.
/FTId=VSP_018685.
MUTAGEN 48 48 A->V: Complete loss of holin function.
{ECO:0000269|PubMed:11029428}.
MUTAGEN 51 51 C->S: No effect on holin function.
{ECO:0000269|PubMed:11029428}.
MUTAGEN 52 52 A->V: Lysis-defective, dimerizes but does
not form cross-linkable oligomers.
{ECO:0000269|PubMed:11029428}.
SEQUENCE 107 AA; 11520 MW; 66D0D62426F1766E CRC64;
MKMPEKHDLL AAILAAKEQG IGAILAFAMA YLRGRYNGGA FTKTVIDATM CAIIAWFIRD
LLDFAGLSSN LAYITSVFIG YIGTDSIGSL IKRFAAKKAG VEDGRNQ


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