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FIB12_BPT4
ID   FIB12_BPT4              Reviewed;         527 AA.
AC   P10930;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   23-FEB-2022, entry version 125.
DE   RecName: Full=Short tail fiber protein gp12;
DE   AltName: Full=Gene product 12;
DE            Short=gp12;
GN   Name=12;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D;
RX   PubMed=3357780; DOI=10.1093/nar/16.5.2334;
RA   Selivanov N.A., Prilipov A.G., Mesyanzhinov V.V.;
RT   "Nucleotide and deduced amino acid sequence of bacteriophage T4 gene 12.";
RL   Nucleic Acids Res. 16:2334-2334(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
RC   STRAIN=D;
RX   PubMed=2548819; DOI=10.1089/dna.1.1989.8.287;
RA   Barrett B.K., Berget P.B.;
RT   "Using transposon Tn5 insertions to sequence bacteriophage T4 gene 11.";
RL   DNA 8:287-295(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
RC   STRAIN=D;
RX   PubMed=2726468; DOI=10.1093/nar/17.8.3303;
RA   Prilipov A.G., Selivanov N.A., Efimov V.P., Marusich E.I.,
RA   Mesyanzhinov V.V.;
RT   "Nucleotide sequences of bacteriophage T4 genes 9, 10 and 11.";
RL   Nucleic Acids Res. 17:3303-3303(1989).
RN   [5]
RP   FUNCTION.
RX   PubMed=12837775; DOI=10.1128/jb.185.14.4022-4030.2003;
RA   Weigele P.R., Scanlon E., King J.;
RT   "Homotrimeric, beta-stranded viral adhesins and tail proteins.";
RL   J. Bacteriol. 185:4022-4030(2003).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 250-527, AND SUBUNIT.
RX   PubMed=11743729; DOI=10.1006/jmbi.2000.5204;
RA   van Raaij M.J., Schoehn G., Burda M.R., Miller S.;
RT   "Crystal structure of a heat and protease-stable part of the bacteriophage
RT   T4 short tail fibre.";
RL   J. Mol. Biol. 314:1137-1146(2001).
RN   [7]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.11 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP   LOCATION, AND FUNCTION.
RX   PubMed=27193680; DOI=10.1038/nature17971;
RA   Taylor N.M., Prokhorov N.S., Guerrero-Ferreira R.C., Shneider M.M.,
RA   Browning C., Goldie K.N., Stahlberg H., Leiman P.G.;
RT   "Structure of the T4 baseplate and its function in triggering sheath
RT   contraction.";
RL   Nature 533:346-352(2016).
CC   -!- FUNCTION: Structural component of the short tail fiber. Adhesion
CC       protein that binds irreversibly to the lipopolysaccharides component
CC       (LPS) on the cell surface of Escherichia coli B strains during virus
CC       attachment. After at least three long tail fibers have bound, short
CC       tail fibers extend and bind irreversibly to the core region of the host
CC       cell LPS. {ECO:0000269|PubMed:12837775, ECO:0000269|PubMed:27193680}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11743729,
CC       ECO:0000269|PubMed:27193680}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:27193680}.
CC   -!- SIMILARITY: Belongs to the tevenvirinae short tail fiber protein
CC       family. {ECO:0000305}.
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DR   EMBL; X06792; CAA29951.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42417.1; -; Genomic_DNA.
DR   EMBL; M26253; AAA32495.1; -; Genomic_DNA.
DR   EMBL; X14192; CAA32398.1; -; Genomic_DNA.
DR   PIR; C32479; C32479.
DR   PIR; S01889; GIBPT4.
DR   RefSeq; NP_049770.1; NC_000866.4.
DR   PDB; 1H6W; X-ray; 1.90 A; A=85-396, B=518-527.
DR   PDB; 1OCY; X-ray; 1.50 A; A=332-527.
DR   PDB; 1PDI; EM; 12.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=250-527.
DR   PDB; 5IV5; EM; 4.11 A; AI/AJ/BA/DB/DC/DD/FE/FF/FG/HH/HI/HJ/O/P/Q/l/m/n=1-527.
DR   PDBsum; 1H6W; -.
DR   PDBsum; 1OCY; -.
DR   PDBsum; 1PDI; -.
DR   PDBsum; 5IV5; -.
DR   SMR; P10930; -.
DR   DrugBank; DB04272; Citric acid.
DR   TCDB; 1.K.1.1.1; the gp27/5 t4-baseplate (t4-bp) family.
DR   GeneID; 1258789; -.
DR   KEGG; vg:1258789; -.
DR   EvolutionaryTrace; P10930; -.
DR   Proteomes; UP000009087; Genome.
DR   GO; GO:0098025; C:virus tail, baseplate; IDA:UniProtKB.
DR   GO; GO:0098024; C:virus tail, fiber; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1340.10; -; 1.
DR   Gene3D; 4.10.1070.10; -; 1.
DR   InterPro; IPR015173; Phage_T4_Gp12.
DR   InterPro; IPR011083; Phage_tail_collar_dom.
DR   InterPro; IPR037053; Phage_tail_collar_dom_sf.
DR   InterPro; IPR027448; Short_tail_fibre_C.
DR   InterPro; IPR044916; Short_tail_fibre_C_sf.
DR   Pfam; PF07484; Collar; 1.
DR   Pfam; PF09089; gp12-short_mid; 1.
DR   Pfam; PF14928; S_tail_recep_bd; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host-virus interaction; Late protein; Reference proteome;
KW   Viral attachment to host cell; Viral attachment to host entry receptor;
KW   Viral tail fiber protein; Viral tail protein; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..527
FT                   /note="Short tail fiber protein gp12"
FT                   /id="PRO_0000165002"
FT   CONFLICT        33
FT                   /note="Q -> H (in Ref. 1; CAA29951 and 2; AAD42417)"
FT                   /evidence="ECO:0000305"
FT   HELIX           247..250
FT                   /evidence="ECO:0007829|PDB:1H6W"
FT   STRAND          257..259
FT                   /evidence="ECO:0007829|PDB:1H6W"
FT   STRAND          264..268
FT                   /evidence="ECO:0007829|PDB:1H6W"
FT   STRAND          276..281
FT                   /evidence="ECO:0007829|PDB:1H6W"
FT   HELIX           335..340
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   STRAND          346..353
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   STRAND          359..364
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   TURN            369..371
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   HELIX           373..378
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   TURN            379..383
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   STRAND          387..391
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   HELIX           407..410
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   HELIX           412..414
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   TURN            425..428
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   STRAND          454..456
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   STRAND          465..467
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   HELIX           493..495
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   HELIX           498..500
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   STRAND          508..510
FT                   /evidence="ECO:0007829|PDB:1OCY"
FT   STRAND          520..524
FT                   /evidence="ECO:0007829|PDB:1OCY"
SQ   SEQUENCE   527 AA;  56205 MW;  F86C7E65205486CC CRC64;
     MSNNTYQHVS NESRYVKFDP TDTNFPPEIT DVQAAIAAIS PAGVNGVPDA SSTTKGILFI
     PTEQEVIDGT NNTKAVTPAT LATRLSYPNA TETVYGLTRY STNDEAIAGV NNESSITPAK
     FTVALNNAFE TRVSTESSNG VIKISSLPQA LAGADDTTAM TPLKTQQLAI KLIAQIAPSE
     TTATESDQGV VQLATVAQVR QGTLREGYAI SPYTFMNSSS TEEYKGVIKL GTQSEVNSNN
     ASVAVTGATL NGRGSTTSMR GVVKLTTTAG SQSGGDASSA LAWNADVIQQ RGGQIIYGTL
     RIEDTFTIAN GGANITGTVR MTGGYIQGNR IVTQNEIDRT IPVGAIMMWA ADSLPSDAWR
     FCHGGTVSAS DCPLYASRIG TRYGGNPSNP GLPDMRGLFV RGSGRGSHLT NPNVNGNDQF
     GKPRLGVGCT GGYVGEVQIQ QMSYHKHAGG FGEHDDLGAF GNTRRSNFVG TRKGLDWDNR
     SYFTNDGYEI DPESQRNSKY TLNRPELIGN ETRPWNISLN YIIKVKE
 
 
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