FIBER_BPSFV
ID FIBER_BPSFV Reviewed; 623 AA.
AC Q9XJP3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2003, sequence version 2.
DT 29-SEP-2021, entry version 82.
DE RecName: Full=Tail spike protein {ECO:0000305};
DE Short=TSP;
DE AltName: Full=Endo-1,3-alpha-L-rhamnosidase {ECO:0000305};
DE EC=3.2.1.- {ECO:0000269|PubMed:12424253, ECO:0000269|PubMed:18462681, ECO:0000269|PubMed:6284};
DE AltName: Full=Endorhamnosidase {ECO:0000305};
OS Shigella phage Sf6 (Shigella flexneri bacteriophage VI) (Bacteriophage
OS SfVI).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Lederbergvirus.
OX NCBI_TaxID=10761;
OH NCBI_TaxID=623; Shigella flexneri.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10439404; DOI=10.1099/13500872-145-7-1649;
RA Chua J.E.H., Manning P.A., Morona R.;
RT "The Shigella flexneri bacteriophage Sf6 tailspike protein
RT (TSP)/endorhamnosidase is related to the bacteriophage P22 TSP and has a
RT motif common to exo- and endoglycanases, and C-5 epimerases.";
RL Microbiology 145:1649-1659(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION TO 240-251, SUBUNIT,
RP AND CATALYTIC ACTIVITY.
RX PubMed=12424253; DOI=10.1074/jbc.m205294200;
RA Freiberg A., Morona R., Van Den Bosch L., Jung C., Behlke J., Carlin N.,
RA Seckler R., Baxa U.;
RT "The tailspike protein of Shigella phage Sf6: a structural homolog of
RT Salmonella phage P22 tailspike protein without sequence similarity in the
RT beta-helix domain.";
RL J. Biol. Chem. 278:1542-1548(2003).
RN [3]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=6284; DOI=10.1111/j.1432-1033.1976.tb10392.x;
RA Iwashita S., Kanegasaki S.;
RT "Enzymic and molecular properties of base-plate parts of bacteriophage
RT P22.";
RL Eur. J. Biochem. 65:87-94(1976).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 110-623, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, MUTAGENESIS OF ASP-248; GLU-294; GLU-367 AND ASP-400,
RP AND ACTIVE SITE.
RX PubMed=18462681; DOI=10.1016/j.str.2008.01.019;
RA Mueller J.J., Barbirz S., Heinle K., Freiberg A., Seckler R., Heinemann U.;
RT "An intersubunit active site between supercoiled parallel beta helices in
RT the trimeric tailspike endorhamnosidase of Shigella flexneri Phage Sf6.";
RL Structure 16:766-775(2008).
CC -!- FUNCTION: Non-covalently bound to the neck of the phage capsid and
CC mediating attachment of the viral particle to host cell-surface
CC polysaccharide. It displays endorhamnosidase enzymatic activity,
CC hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and
CC galactose of the O-antigen polysaccharide.
CC {ECO:0000269|PubMed:18462681, ECO:0000305|PubMed:12424253,
CC ECO:0000305|PubMed:6284}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:6284};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12424253,
CC ECO:0000269|PubMed:18462681}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:6284}.
CC -!- DOMAIN: The active site involves residues located on two different
CC subunits. {ECO:0000269|PubMed:18462681}.
CC -!- SIMILARITY: Belongs to the P22likevirus tail fiber protein family.
CC {ECO:0000305}.
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DR EMBL; AF128887; AAD33394.2; -; Genomic_DNA.
DR PDB; 2VBE; X-ray; 1.98 A; A=110-623.
DR PDB; 2VBK; X-ray; 1.25 A; A=110-623.
DR PDB; 2VBM; X-ray; 2.00 A; A=110-623.
DR PDB; 4URR; X-ray; 1.95 A; A/B/C/D/E/F=110-623.
DR PDBsum; 2VBE; -.
DR PDBsum; 2VBK; -.
DR PDBsum; 2VBM; -.
DR PDBsum; 4URR; -.
DR SMR; Q9XJP3; -.
DR DIP; DIP-29798N; -.
DR UniLectin; Q9XJP3; -.
DR EvolutionaryTrace; Q9XJP3; -.
DR GO; GO:0098024; C:virus tail, fiber; IDA:UniProtKB.
DR GO; GO:0052775; F:endo-1,3-alpha-L-rhamnosidase activity; IDA:UniProtKB.
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 Gene3D; 2.170.14.10; -; 1.
DR InterPro; IPR009093; P22_tailspike_N.
DR InterPro; IPR036730; P22_tailspike_N_sf.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF09008; Head_binding; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR SUPFAM; SSF51327; SSF51327; 1.
PE 1: Evidence at protein level;
KW 3D-structure;
KW Degradation of host cell envelope components during virus entry;
KW Degradation of host lipopolysaccharides during virus entry; Glycosidase;
KW Host-virus interaction; Hydrolase; Viral attachment to host cell;
KW Viral tail fiber protein; Viral tail protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..623
FT /note="Tail spike protein"
FT /id="PRO_0000077758"
FT ACT_SITE 367
FT /note="Shared with dimeric partner"
FT /evidence="ECO:0000269|PubMed:18462681"
FT ACT_SITE 400
FT /note="Shared with dimeric partner"
FT /evidence="ECO:0000269|PubMed:18462681"
FT SITE 248
FT /note="Substrate binding"
FT /evidence="ECO:0000269|PubMed:18462681"
FT SITE 294
FT /note="Substrate binding"
FT /evidence="ECO:0000269|PubMed:18462681"
FT MUTAGEN 248
FT /note="D->N: 98.5% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18462681"
FT MUTAGEN 294
FT /note="E->Q: 87% loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18462681"
FT MUTAGEN 367
FT /note="E->Q: Almost complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18462681"
FT MUTAGEN 400
FT /note="D->N: Almost complete loss of enzymatic activity."
FT /evidence="ECO:0000269|PubMed:18462681"
FT HELIX 114..123
FT /evidence="ECO:0007829|PDB:2VBK"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:2VBK"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2VBK"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:2VBK"
FT HELIX 163..166
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:2VBK"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 263..271
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 291..311
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 313..325
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:2VBK"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 367..379
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 390..410
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 413..425
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 434..438
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 448..456
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 507..510
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 553..558
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 565..570
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:2VBK"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 594..598
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:2VBK"
FT STRAND 616..622
FT /evidence="ECO:0007829|PDB:2VBK"
SQ SEQUENCE 623 AA; 67066 MW; 481FA9C23C349A9B CRC64;
MTDIITNVVI GMPSQLFTMA RSFKAVANGK IYIGKIDTDP VNPENQIQVY VENEDGSHVP
ASQPIVINAA GYPVYNGQIV KFVTEQGHSM AVYDAYGSQQ FYFQNVLKYD PDQFGPDLIE
QLAQSGKYSQ DNTKGDAMIG VKQPLPKAVL RTQHDKNKEA ISILDFGVID DGVTDNYQAI
QNAIDAVASL PSGGELFIPA SNQAVGYIVG STLLIPGGVN IRGVGKASQL RAKSGLTGSV
LRLSYDSDTI GRYLRNIRVT GNNTCNGIDT NITAEDSVIR QVYGWVFDNV MVNEVETAYL
MQGLWHSKFI ACQAGTCRVG LHFLGQCVSV SVSSCHFSRG NYSADESFGI RIQPQTYAWS
SEAVRSEAII LDSETMCIGF KNAVYVHDCL DLHMEQLDLD YCGSTGVVIE NVNGGFSFSN
SWIAADADGT EQFTGIYFRT PTSTQSHKIV SGVHINTANK NTAANNQSIA IEQSAIFVFV
SGCTLTGDEW AVNIVDINEC VSFDKCIFNK PLRYLRSGGV SVTDCYLAGI TEVQKPEGRY
NTYRGCSGVP SVNGIINVPV AVGATSGSAA IPNPGNLTYR VRSLFGDPAS SGDKVSVSGV
TINVTRPSPV GVALPSMVEY LAI
