ID   FIBER_BPE15             Reviewed;        1070 AA.
AC   Q858F5;
DT   29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Tail spike protein {ECO:0000305};
DE            Short=TSP;
DE   AltName: Full=Endorhamnosidase {ECO:0000305};
DE            EC=3.2.1.-;
DE   AltName: Full=Gene product 20 {ECO:0000305};
DE            Short=gp20;
OS   Salmonella phage epsilon15.
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Podoviridae; Uetakevirus.
OX   NCBI_TaxID=215158 {ECO:0000312|Proteomes:UP000001770};
OH   NCBI_TaxID=58712; Salmonella anatum.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17825342; DOI=10.1016/j.virol.2007.07.027;
RA   Kropinski A.M., Kovalyova I.V., Billington S.J., Patrick A.N., Butts B.D.,
RA   Guichard J.A., Pitcher T.J., Guthrie C.C., Sydlaske A.D., Barnhill L.M.,
RA   Havens K.A., Day K.R., Falk D.R., McConnell M.R.;
RT   "The genome of epsilon15, a serotype-converting, Group E1 Salmonella
RT   enterica-specific bacteriophage.";
RL   Virology 369:234-244(2007).
RN   [2]
RP   FUNCTION.
RX   PubMed=4633001; DOI=10.1016/0042-6822(73)90405-4;
RA   Takeda K., Uetake H.;
RT   "In vitro interaction between phage and receptor lipopolysaccharide: a
RT   novel glycosidase associated with Salmonella phage 15.";
RL   Virology 52:148-159(1973).
RN   [3]
RP   STRUCTURE BY ELECTRON MICROSCOPY (9.5 ANGSTROMS) OF THE VIRAL PARTICLE,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16452981; DOI=10.1038/nature04487;
RA   Jiang W., Chang J., Jakana J., Weigele P., King J., Chiu W.;
RT   "Structure of epsilon15 bacteriophage reveals genome organization and DNA
RT   packaging/injection apparatus.";
RL   Nature 439:612-616(2006).
RN   [4]
RP   FUNCTION.
RX   PubMed=20709082; DOI=10.1016/j.jmb.2010.07.058;
RA   Chang J.T., Schmid M.F., Haase-Pettingell C., Weigele P.R., King J.A.,
RA   Chiu W.;
RT   "Visualizing the structural changes of bacteriophage Epsilon15 and its
RT   Salmonella host during infection.";
RL   J. Mol. Biol. 402:731-740(2010).
CC   -!- FUNCTION: Structural component of the short non-contractile tail
CC       (PubMed:16452981). The tail comprises six spikes that mediate primary
CC       attachment to the host cell lipopolysaccharides (LPS) and display
CC       endorhamnosidase enzymatic activity, hydrolyzing the linkage between
CC       rhamnose and galactose of the O-antigen polysaccharide. Digestion of
CC       the LPS brings the capsid near the cell outer membrane
CC       (PubMed:20709082, PubMed:4633001). {ECO:0000269|PubMed:16452981,
CC       ECO:0000269|PubMed:20709082, ECO:0000269|PubMed:4633001}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16452981}.
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DR   EMBL; AY150271; AAO06083.1; -; Genomic_DNA.
DR   RefSeq; NP_848228.1; NC_004775.1.
DR   SMR; Q858F5; -.
DR   PRIDE; Q858F5; -.
DR   GeneID; 2641857; -.
DR   KEGG; vg:2641857; -.
DR   Proteomes; UP000001770; Genome.
DR   GO; GO:0098024; C:virus tail, fiber; IDA:UniProtKB.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IDA:UniProtKB.
DR   GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0098995; P:disruption by virus of host envelope lipopolysaccharide during virus entry; IEA:UniProtKB-KW.
DR   GO; GO:0044409; P:entry into host; IDA:UniProtKB.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IDA:UniProtKB.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Pfam; PF13229; Beta_helix; 1.
DR   SMART; SM00710; PbH1; 5.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   1: Evidence at protein level;
KW   Degradation of host cell envelope components during virus entry;
KW   Degradation of host lipopolysaccharides during virus entry; Glycosidase;
KW   Host-virus interaction; Hydrolase; Late protein; Reference proteome;
KW   Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW   Viral tail fiber protein; Viral tail protein; Virion;
KW   Virus entry into host cell.
FT   CHAIN           1..1070
FT                   /note="Tail spike protein"
FT                   /id="PRO_0000432954"
SQ   SEQUENCE   1070 AA;  115676 MW;  5184A1E5BDA3BA07 CRC64;
     MTVSTEVDHN DYTGNGVTTS FPYTFRIFKK SDLVVQVVDL NENITELILD TDYTVTGAGG
     YTCGDVVLSS PLANGYQISI SRELPVTQET DLRNQGKFFA EVHENAFDKL TMLIQQVRSW
     LSLALRKPSF VANYYDALGN YIRNLRDPSR PQDAATKNYV DNLSEGNNSY ADNLFSRTLR
     VPEKINTLPS SLDRANKIPA FDSNGNAIVI IPQSGSASDV LIELAKPSGS GLVGFSHSNN
     YNPGMVGEKL QNVVYPTDAP FYAPTDGTSD ATTALQSAIT HCEGKNAVLC INKSFSVSDS
     LSISSPLCVF AMNEQCGIVS SAPAGHAAVI FNGDNICWNG GFIRGLNQPS SSTIRQDGVL
     LNGNDCVLDN VSINGFFAKG LHTSNADGSG VGIRDYGTRN TISKCRVEYN KFGISLEGKD
     GWVLGNYVSN HYRMSSEAKP WDDTSNYWDG IVGGGEWLGV ATGYLIDGNE FEDNGQSGIY
     AGGNGGIFAK NRITNNHIHG NWNRGIDFGV VQRLANSDVY ENIITDNIVH NNRAANIWLA
     GVRDSIINNN NSWFTDDYRS MFAGNFDACV CLTLADGGEK AAPTGNQVNG NRCKTLESDD
     QISGFTLNIT DTARGNQVRD NVLSPIGEAY IPNPELYAVN NIDIPTEFAF TPQLIGGSGV
     TLGNSSGKLT ANGNVFSLSL SISAQSVSSP SGSLTIGYIP GLSGTSVRHH NVRTEFYNNL
     NTTMQRAQPY VNIGDSADQL RVYRLADGLS KDDLLEYFMS NSDLRMVGDI EIEPYNFSRS
     VTVVGHSFCT SDVMSTELNR LLGTDIYNFA RGGASDVEVA MSQEAITRQY APVGGSIPAS
     GSVALTPTEV GIFWNGATGK CIFGGIDGTF STTLVNAGTG ETQLVFTRDS AGSAVSVSTT
     ATFAMRPYTR FNTNTIPAGR KHSLHRDDIY IVWGGRNSTD YTRYVSELHT MVANMHTQRF
     VICPEFPYDT ETTGTTGATN LAALNNNLKA DFPDNYCQIS GVDLLQNFKS KYNPAYAGDV
     TDIANGITPR SLREDNLHPS ETLQPNGLYI GAKVNADFIA QFIKSKGWGG