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HOLIN_BPMD2
ID   HOLIN_BPMD2             Reviewed;         141 AA.
AC   O64204;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   23-FEB-2022, entry version 46.
DE   RecName: Full=Holin {ECO:0000255|HAMAP-Rule:MF_04168, ECO:0000303|PubMed:26471254};
DE   AltName: Full=Gene product 11 {ECO:0000305};
DE            Short=gp11 {ECO:0000305};
GN   Name=11;
OS   Mycobacterium phage D29 (Mycobacteriophage D29).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Fromanvirus.
OX   NCBI_TaxID=28369;
OH   NCBI_TaxID=1763; Mycobacterium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9636706; DOI=10.1006/jmbi.1997.1610;
RA   Ford M.E., Sarkis G.J., Belanger A.E., Hendrix R.W., Hatfull G.F.;
RT   "Genome structure of mycobacteriophage D29: implications for phage
RT   evolution.";
RL   J. Mol. Biol. 279:143-164(1998).
RN   [2]
RP   FUNCTION, MUTAGENESIS OF GLY-28, AND DOMAIN.
RX   PubMed=26471254; DOI=10.1111/febs.13565;
RA   Kamilla S., Jain V.;
RT   "Mycobacteriophage D29 holin C-terminal region functionally assists in
RT   holin aggregation and bacterial cell death.";
RL   FEBS J. 283:173-190(2016).
RN   [3]
RP   DOMAIN, MUTAGENESIS OF 17-PRO-GLY-18, AND SUBUNIT.
RX   PubMed=26701742; DOI=10.1021/acschembio.5b00875;
RA   Lella M., Kamilla S., Jain V., Mahalakshmi R.;
RT   "Molecular Mechanism of Holin Transmembrane Domain I in Pore Formation and
RT   Bacterial Cell Death.";
RL   ACS Chem. Biol. 11:910-920(2016).
RN   [4]
RP   FUNCTION.
RX   PubMed=32477303; DOI=10.3389/fmicb.2020.00883;
RA   Bavda V.R., Jain V.;
RT   "Deciphering the Role of Holin in Mycobacteriophage D29 Physiology.";
RL   Front. Microbiol. 11:883-883(2020).
RN   [5]
RP   DOMAIN.
RX   PubMed=33627396; DOI=10.1128/jvi.02173-20;
RA   Bavda V.R., Yadav A., Jain V.;
RT   "Decoding the molecular properties of mycobacteriophage D29 Holin provides
RT   insights into Holin engineering.";
RL   J. Virol. 0:0-0(2021).
CC   -!- FUNCTION: Accumulates harmlessly in the cytoplasmic membrane until it
CC       reaches a critical concentration that triggers the formation of micron-
CC       scale pores (holes) causing host cell membrane disruption and endolysin
CC       escape into the periplasmic space (Probable). Determines the precise
CC       timing of host cell lysis (PubMed:32477303). Participates with the
CC       endolysin protein in the sequential events which lead to the programmed
CC       host cell lysis releasing the mature viral particles from the host cell
CC       (PubMed:26471254). {ECO:0000255|HAMAP-Rule:MF_04168,
CC       ECO:0000269|PubMed:26471254, ECO:0000269|PubMed:32477303, ECO:0000305}.
CC   -!- SUBUNIT: Homomultimer (PubMed:26701742). Self-associates to form a pore
CC       (PubMed:26701742). {ECO:0000255|HAMAP-Rule:MF_04168,
CC       ECO:0000269|PubMed:26701742}.
CC   -!- SUBCELLULAR LOCATION: Host cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04168}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04168, ECO:0000305}.
CC   -!- DOMAIN: The first transmembrane region undergoes a helix to beta-
CC       hairpin conformational change, which is responsible for its self-
CC       association and pore formation in the host membrane (PubMed:26701742).
CC       The coiled coil region is required for host cell lysis and for
CC       cytotoxic activity (PubMed:33627396, PubMed:26471254). The C-terminus
CC       determines the size of the hole (PubMed:26471254). {ECO:0000255|HAMAP-
CC       Rule:MF_04168, ECO:0000269|PubMed:26471254,
CC       ECO:0000269|PubMed:26701742, ECO:0000269|PubMed:33627396}.
CC   -!- SIMILARITY: Belongs to the Mycobacterium phage D29 holin family.
CC       {ECO:0000255|HAMAP-Rule:MF_04168}.
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DR   EMBL; AF022214; AAC18451.1; -; Genomic_DNA.
DR   PIR; H72800; H72800.
DR   RefSeq; NP_046826.1; NC_001900.1.
DR   SMR; O64204; -.
DR   TCDB; 1.E.36.1.7; the mycobacterial 2 tms phage holin (m2 hol) family.
DR   GeneID; 1261605; -.
DR   KEGG; vg:1261605; -.
DR   Proteomes; UP000002131; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0044660; P:viral release by cytolysis via pore formation in host cell membrane; IMP:UniProtKB.
DR   HAMAP; MF_04168; HOLIN_D29; 1.
DR   InterPro; IPR032121; Myco_phage_holin.
DR   Pfam; PF16081; Phage_holin_7_1; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytolysis; Host cell inner membrane; Host cell lysis by virus;
KW   Host cell membrane; Host membrane; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Viral release from host cell.
FT   CHAIN           1..141
FT                   /note="Holin"
FT                   /id="PRO_0000164710"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04168"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04168"
FT   COILED          74..108
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04168"
FT   MUTAGEN         17..18
FT                   /note="PG->AA: Decreased and delayed host membrane
FT                   disruption."
FT                   /evidence="ECO:0000269|PubMed:26701742"
FT   MUTAGEN         28
FT                   /note="G->D: Complete loss of ability to induce host cell
FT                   lysis."
FT                   /evidence="ECO:0000269|PubMed:26471254"
SQ   SEQUENCE   141 AA;  14618 MW;  0A4E0279E8D7A04B CRC64;
     MSPKIRETLY YVGTLVPGIL GIALIWGGID AGAAANIGDI VAGALNLVGA AAPATAAVKV
     NQQRKDGTLT TSPVDQVTRG VEQVLAAKQN AEAEVERVKQ ALESAVNGAV PQLGPLASQI
     LNGIQPAYSQ PFDPHTQPWN R
 
 
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