位置:首页 > 蛋白库 > NEEDL_BPP22
NEEDL_BPP22
ID   NEEDL_BPP22             Reviewed;         233 AA.
AC   P35837; I7KJL6; Q8LTG5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-JUN-2021, entry version 91.
DE   RecName: Full=Tail needle protein gp26;
DE   AltName: Full=Head completion protein;
DE   AltName: Full=Packaged DNA stabilization protein;
DE   AltName: Full=Tail accessory factor gp26;
GN   Name=26;
OS   Salmonella phage P22 (Bacteriophage P22).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Podoviridae; Lederbergvirus.
OX   NCBI_TaxID=10754;
OH   NCBI_TaxID=90371; Salmonella typhimurium.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8341611; DOI=10.1093/nar/21.14.3326;
RA   Casjens S.R., Sampson L.;
RT   "Nucleotide sequence of Salmonella bacteriophage P22 head completion genes
RT   10 and 26.";
RL   Nucleic Acids Res. 21:3326-3326(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11053393; DOI=10.1128/jb.182.22.6472-6481.2000;
RA   Vander Byl C.S., Kropinski A.M.B.;
RT   "Sequence of the genome of Salmonella bacteriophage P22.";
RL   J. Bacteriol. 182:6472-6481(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12562822; DOI=10.1128/jb.185.4.1475-1477.2003;
RA   Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W.,
RA   Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A.,
RA   Casjens S.R.;
RT   "Corrected sequence of the bacteriophage P22 genome.";
RL   J. Bacteriol. 185:1475-1477(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=20817910; DOI=10.1074/jbc.m110.169003;
RA   Andres D., Hanke C., Baxa U., Seul A., Barbirz S., Seckler R.;
RT   "Tailspike interactions with lipopolysaccharide effect DNA ejection from
RT   phage P22 particles in vitro.";
RL   J. Biol. Chem. 285:36768-36775(2010).
RN   [5]
RP   FUNCTION.
RX   PubMed=30886360; DOI=10.1038/s41564-019-0403-z;
RA   Wang C., Tu J., Liu J., Molineux I.J.;
RT   "Structural dynamics of bacteriophage P22 infection initiation revealed by
RT   cryo-electron tomography.";
RL   Nat. Microbiol. 4:1049-1056(2019).
RN   [6]
RP   ELECTRON MICROSCOPY (20 ANGSTROMS) OF COMPLETE VIRION, AND SUBUNIT.
RX   PubMed=16730179; DOI=10.1016/j.str.2006.05.007;
RA   Chang J., Weigele P., King J., Chiu W., Jiang W.;
RT   "Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals
RT   organization of its DNA packaging and infecting machinery.";
RL   Structure 14:1073-1082(2006).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT, AND FUNCTION.
RX   PubMed=18059287; DOI=10.1038/nsmb1317;
RA   Olia A.S., Casjens S., Cingolani G.;
RT   "Structure of phage P22 cell envelope-penetrating needle.";
RL   Nat. Struct. Mol. Biol. 14:1221-1226(2007).
CC   -!- FUNCTION: Cell-perforating component and plug protein of the phage tail
CC       machine (PubMed:18059287, PubMed:20817910). Together with gp4 and gp10,
CC       gp26 is required for stabilization of the condensed DNA within the
CC       capsid by plugging the hole through which the DNA enters
CC       (PubMed:18059287). Host cell membrane perforation allows viral DNA
CC       ejection (PubMed:18059287). The needle penetrates the host outer
CC       membrane. The needle is released and the internal head protein gp7 is
CC       ejected to form an extra-cellular channel (PubMed:30886360).
CC       {ECO:0000269|PubMed:18059287, ECO:0000269|PubMed:20817910,
CC       ECO:0000269|PubMed:30886360}.
CC   -!- SUBUNIT: Elongated coiled-coil homotrimer (240A x 25A). Interacts with
CC       gp10. {ECO:0000269|PubMed:16730179, ECO:0000269|PubMed:18059287}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L14810; AAA32271.1; -; Genomic_DNA.
DR   EMBL; AF217253; AAF75051.1; -; Genomic_DNA.
DR   EMBL; AF527608; AAM81393.1; -; Genomic_DNA.
DR   EMBL; BK000583; DAA00991.1; -; Genomic_DNA.
DR   PIR; S34956; S34956.
DR   RefSeq; YP_063715.1; NC_002371.2.
DR   PDB; 2POH; X-ray; 2.10 A; A/B/C/D/E/F=1-233.
DR   PDB; 3C9I; X-ray; 1.95 A; A/B/C/D/E/F=1-233.
DR   PDB; 4LIN; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L=1-233.
DR   PDB; 4ZKP; X-ray; 2.10 A; A/B=1-233.
DR   PDB; 4ZKU; X-ray; 2.50 A; A/B=1-233.
DR   PDB; 4ZXQ; X-ray; 2.75 A; A/B/C/D/E/F=1-140.
DR   PDBsum; 2POH; -.
DR   PDBsum; 3C9I; -.
DR   PDBsum; 4LIN; -.
DR   PDBsum; 4ZKP; -.
DR   PDBsum; 4ZKU; -.
DR   PDBsum; 4ZXQ; -.
DR   SMR; P35837; -.
DR   DIP; DIP-60502N; -.
DR   TCDB; 1.K.4.1.1; the phage p22 injectisome (p22 injectisome) family.
DR   GeneID; 2944243; -.
DR   KEGG; vg:2944243; -.
DR   EvolutionaryTrace; P35837; -.
DR   Proteomes; UP000001795; Genome.
DR   Proteomes; UP000001796; Genome.
DR   Proteomes; UP000007960; Genome.
DR   GO; GO:0098015; C:virus tail; IEA:UniProtKB-KW.
DR   GO; GO:0044694; P:pore-mediated entry of viral genome into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0099002; P:viral genome ejection through host cell envelope, short tail mechanism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Late protein;
KW   Pore-mediated penetration of viral genome into host cell;
KW   Reference proteome; Repeat;
KW   Viral genome ejection through host cell envelope;
KW   Viral penetration into host cytoplasm; Viral short tail ejection system;
KW   Viral tail protein; Virion; Virus entry into host cell.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000305"
FT   CHAIN           2..233
FT                   /note="Tail needle protein gp26"
FT                   /id="PRO_0000077767"
FT   REPEAT          77..84
FT                   /note="Trimerization octad repeat 1"
FT   REPEAT          98..105
FT                   /note="Trimerization octad repeat 2"
FT   REPEAT          112..119
FT                   /note="Trimerization octad repeat 3"
FT   REPEAT          133..140
FT                   /note="Trimerization octad repeat 4"
FT   REPEAT          205..212
FT                   /note="Trimerization octad repeat 5"
FT   REGION          2..27
FT                   /note="Interaction with gp10"
FT   REGION          28..140
FT                   /note="Fibrous core"
FT   REGION          141..170
FT                   /note="Beta-helix"
FT   REGION          171..233
FT                   /note="Lazo"
FT   MOTIF           216..220
FT                   /note="Basic cluster"
FT   SITE            200
FT                   /note="Needle distal tip"
FT   CONFLICT        169
FT                   /note="L -> V (in Ref. 3; AAM81393/DAA00991)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..7
FT                   /evidence="ECO:0007829|PDB:3C9I"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:3C9I"
FT   TURN            24..26
FT                   /evidence="ECO:0007829|PDB:3C9I"
FT   HELIX           29..139
FT                   /evidence="ECO:0007829|PDB:3C9I"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:3C9I"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:3C9I"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:3C9I"
FT   STRAND          166..169
FT                   /evidence="ECO:0007829|PDB:3C9I"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:4LIN"
FT   HELIX           202..229
FT                   /evidence="ECO:0007829|PDB:3C9I"
FT   STRAND          230..232
FT                   /evidence="ECO:0007829|PDB:2POH"
SQ   SEQUENCE   233 AA;  24734 MW;  B4564B274B5564D3 CRC64;
     MADPSLNNPV VIQATRLDAS ILPRNVFSKS YLLYVIAQGT DVGAIAGKAN EAGQGAYDAQ
     VKNDEQDVEL ADHEARIKQL RIDVDDHESR ITANTKAITA LNVRVTTAEG EIASLQTNVS
     ALDGRVTTAE NNISALQADY VSKTATTSQS LASPLNVTTS YSVGGKKVLG ARQTGWTAAT
     GTANKGVFDA DLTFAVSDTY TQSEIQAIAN ALITERRRTK ALEDALRAHG LID
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025