HOLIN_LAMBD
ID HOLIN_LAMBD Reviewed; 107 AA.
AC P03705;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 07-APR-2021, entry version 115.
DE RecName: Full=Antiholin {ECO:0000303|PubMed:8878031};
DE AltName: Full=Lysis inhibitor S-107 {ECO:0000303|PubMed:8878031};
GN Name=S;
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 MUTAGENESIS.
RX PubMed=2943725; DOI=10.1128/jb.167.3.1035-1042.1986;
RA Raab R., Neal G., Garrett J., Grimaila R., Fusselman R., Young R.;
RT "Mutational analysis of bacteriophage lambda lysis gene S.";
RL J. Bacteriol. 167:1035-1042(1986).
RN [3]
RP FUNCTION, AND ALTERNATIVE INITIATION.
RX PubMed=8878031; DOI=10.1046/j.1365-2958.1996.331395.x;
RA Blasi U., Young R.;
RT "Two beginnings for a single purpose: the dual-start holins in the
RT regulation of phage lysis.";
RL Mol. Microbiol. 21:675-682(1996).
RN [4]
RP TOPOLOGY.
RX PubMed=10217787; DOI=10.1128/jb.181.9.2922-2929.1999;
RA Blasi U., Fraisl P., Chang C.Y., Zhang N., Young R.;
RT "The C-terminal sequence of the lambda holin constitutes a cytoplasmic
RT regulatory domain.";
RL J. Bacteriol. 181:2922-2929(1999).
RN [5]
RP FUNCTION (ISOFORM ANTIHOLIN), AND ALTERNATIVE INITIATION.
RX PubMed=2138979; DOI=10.1002/j.1460-2075.1990.tb08200.x;
RA Blasi U., Chang C.Y., Zagotta M.T., Nam K.B., Young R.;
RT "The lethal lambda S gene encodes its own inhibitor.";
RL EMBO J. 9:981-989(1990).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=2137120; DOI=10.1128/jb.172.2.912-921.1990;
RA Zagotta M.T., Wilson D.B.;
RT "Oligomerization of the bacteriophage lambda S protein in the inner
RT membrane of Escherichia coli.";
RL J. Bacteriol. 172:912-921(1990).
RN [7]
RP INTERACTION WITH ISOFORM ANTIHOLIN (ISOFORM HOLIN).
RX PubMed=11029427; DOI=10.1128/jb.182.21.6075-6081.2000;
RA Grundling A., Smith D.L., Blasi U., Young R.;
RT "Dimerization between the holin and holin inhibitor of phage lambda.";
RL J. Bacteriol. 182:6075-6081(2000).
RN [8]
RP SUBUNIT, AND MUTAGENESIS OF ALA-48; CYS-51 AND ALA-52.
RX PubMed=11029428; DOI=10.1128/jb.182.21.6082-6090.2000;
RA Grundling A., Blasi U., Young R.;
RT "Genetic and biochemical analysis of dimer and oligomer interactions of the
RT lambda S holin.";
RL J. Bacteriol. 182:6082-6090(2000).
RN [9]
RP FUNCTION (ISOFORM HOLIN).
RX PubMed=18788120; DOI=10.1111/j.1365-2958.2008.06298.x;
RA Savva C.G., Dewey J.S., Deaton J., White R.L., Struck D.K., Holzenburg A.,
RA Young R.;
RT "The holin of bacteriophage lambda forms rings with large diameter.";
RL Mol. Microbiol. 69:784-793(2008).
RN [10]
RP TOPOLOGY, AND FORMYLATION AT MET-1 (ISOFORM HOLIN).
RX PubMed=19897658; DOI=10.1128/jb.01263-09;
RA White R., Tran T.A., Dankenbring C.A., Deaton J., Young R.;
RT "The N-terminal transmembrane domain of lambda S is required for holin but
RT not antiholin function.";
RL J. Bacteriol. 192:725-733(2010).
RN [11]
RP FUNCTION (ISOFORM HOLIN), AND FUNCTION (ISOFORM ANTIHOLIN).
RX PubMed=21187415; DOI=10.1073/pnas.1011921108;
RA White R., Chiba S., Pang T., Dewey J.S., Savva C.G., Holzenburg A.,
RA Pogliano K., Young R.;
RT "Holin triggering in real time.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:798-803(2011).
RN [12]
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).
CC -!- FUNCTION: [Isoform Holin]: Accumulates harmlessly in the cytoplasmic
CC membrane until it reaches a critical concentration that triggers the
CC formation of micron-scale pores (holes) causing host cell membrane
CC disruption and endolysin escape into the periplasmic space
CC (PubMed:18788120, PubMed:21187415). Determines the precise timing of
CC host cell lysis (PubMed:21187415). Participates with the endolysin and
CC spanin proteins in the sequential events which lead to the programmed
CC host cell lysis releasing the mature viral particles from the host cell
CC (PubMed:21187415). {ECO:0000269|PubMed:18788120,
CC ECO:0000269|PubMed:21187415}.
CC -!- FUNCTION: [Isoform Antiholin]: Counteracts the aggregation of the holin
CC molecules and thus of pore formation. {ECO:0000269|PubMed:21187415,
CC ECO:0000269|PubMed:2138979}.
CC -!- SUBUNIT: [Isoform Holin]: Homomultimer (PubMed:11029428). Interacts
CC with isoform Antiholin; this interaction blocks the holin
CC homomultimerization and delays host cell lysis (PubMed:11029427).
CC {ECO:0000269|PubMed:11029427, ECO:0000269|PubMed:11029428}.
CC -!- SUBCELLULAR LOCATION: Host cell inner membrane
CC {ECO:0000269|PubMed:2137120}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19897658}. Note=Classified as a class I holin.
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Antiholin; Synonyms=Lysis inhibitor S-107
CC {ECO:0000303|PubMed:2138979, ECO:0000303|PubMed:8878031};
CC IsoId=P03705-1; Sequence=Displayed;
CC Name=Holin {ECO:0000303|PubMed:8878031}; Synonyms=Lysis protein S-105
CC {ECO:0000303|PubMed:2138979, ECO:0000303|PubMed:8878031};
CC IsoId=P03705-2; Sequence=VSP_018685;
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC -!- DOMAIN: [Isoform Holin]: Has 3 transmembrane regions whereas isoform
CC Antiholin lacks the first transmembrane region.
CC {ECO:0000269|PubMed:19897658}.
CC -!- DOMAIN: The C-terminus acts as a cytoplasmic regulatory region.
CC -!- SIMILARITY: Belongs to the lambdavirus holin family. {ECO:0000305}.
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DR EMBL; J02459; AAA96597.1; -; Genomic_DNA.
DR EMBL; M14035; AAA32248.1; -; Genomic_DNA.
DR PIR; H94164; YVBPL.
DR RefSeq; NP_040644.1; NC_001416.1. [P03705-1]
DR RefSeq; YP_001551775.1; NC_001416.1. [P03705-2]
DR IntAct; P03705; 3.
DR TCDB; 1.E.2.1.1; the Lambda holin s (Lambda holin) family.
DR GeneID; 2703479; -.
DR GeneID; 5740919; -.
DR KEGG; vg:2703479; -.
DR KEGG; vg:5740919; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0020002; C:host cell plasma membrane; IDA:CACAO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034291; F:canonical holin activity; IMP:CACAO.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0045918; P:negative regulation of cytolysis; IDA:CACAO.
DR GO; GO:0044659; P:viral release from host cell by cytolysis; IDA:UniProtKB.
DR InterPro; IPR006481; Phage_lambda_GpS_holin.
DR Pfam; PF05106; Phage_holin_3_1; 1.
DR TIGRFAMs; TIGR01594; holin_lambda; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cytolysis; Formylation; Host cell inner membrane;
KW Host cell lysis by virus; Host cell membrane; Host membrane; Late protein;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral release from host cell.
FT CHAIN 1..107
FT /note="Antiholin"
FT /id="PRO_0000003370"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19897658"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..70
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:19897658"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:10217787"
FT VAR_SEQ 1..2
FT /note="Missing (in isoform Holin)"
FT /evidence="ECO:0000269|PubMed:2138979,
FT ECO:0000269|PubMed:8878031"
FT /id="VSP_018685"
FT MUTAGEN 48
FT /note="A->V: Complete loss of holin function."
FT /evidence="ECO:0000269|PubMed:11029428"
FT MUTAGEN 51
FT /note="C->S: No effect on holin function."
FT /evidence="ECO:0000269|PubMed:11029428"
FT MUTAGEN 52
FT /note="A->V: Lysis-defective, dimerizes but does not form
FT cross-linkable oligomers."
FT /evidence="ECO:0000269|PubMed:11029428"
FT TOPO_DOM P03705-2:1..6
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:19897658"
FT TRANSMEM P03705-2:7..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM P03705-2:27..35
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:19897658"
FT MOD_RES P03705-2:1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:19897658"
SQ SEQUENCE 107 AA; 11520 MW; 66D0D62426F1766E CRC64;
MKMPEKHDLL AAILAAKEQG IGAILAFAMA YLRGRYNGGA FTKTVIDATM CAIIAWFIRD
LLDFAGLSSN LAYITSVFIG YIGTDSIGSL IKRFAAKKAG VEDGRNQ
