FIBER_BPP22
ID FIBER_BPP22 Reviewed; 667 AA.
AC P12528; Q7PCJ1;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 23-FEB-2022, entry version 140.
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:383902, ECO:0000269|PubMed:8889178};
DE AltName: Full=Endorhamnosidase {ECO:0000305};
DE AltName: Full=Gene product 9 {ECO:0000305};
DE Short=gp9;
GN Name=9;
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=6295443; DOI=10.1021/bi00266a014;
RA Sauer R.T., Krovatin W., Poteete A.R., Berget P.B.;
RT "Phage P22 tail protein: gene and amino acid sequence.";
RL Biochemistry 21:5811-5815(1982).
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 CATALYTIC ACTIVITY.
RX PubMed=383902; DOI=10.1099/0022-1317-43-3-503;
RA Eriksson U., Svenson S.B., Loenngren J., Lindberg A.A.;
RT "Salmonella phage glycanases: substrate specificity of the phage P22 endo-
RT rhamnosidase.";
RL J. Gen. Virol. 43:503-511(1979).
RN [5]
RP ACTIVE SITE, MUTAGENESIS OF GLU-360; ASP-393 AND ASP-396, AND CATALYTIC
RP ACTIVITY.
RX PubMed=8889178; DOI=10.1016/s0006-3495(96)79402-x;
RA Baxa U., Steinbacher S., Miller S., Weintraub A., Huber R., Seckler R.;
RT "Interactions of phage P22 tails with their cellular receptor, Salmonella
RT O-antigen polysaccharide.";
RL Biophys. J. 71:2040-2048(1996).
RN [6]
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 [7]
RP FUNCTION, AND INTERACTION WITH HOST LIPOPOLYSACCHARIDES.
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 110-667.
RX PubMed=8023158; DOI=10.1126/science.8023158;
RA Steinbacher S., Seckler R., Miller S., Steipe B., Huber R., Reinemer P.;
RT "Crystal structure of P22 tailspike protein: interdigitated subunits in a
RT thermostable trimer.";
RL Science 265:383-386(1994).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 110-667 IN COMPLEX WITH O-ANTIGEN.
RX PubMed=8855221; DOI=10.1073/pnas.93.20.10584;
RA Steinbacher S., Baxa U., Miller S., Weintraub A., Seckler R., Huber R.;
RT "Crystal structure of phage P22 tailspike protein complexed with Salmonella
RT sp. O-antigen receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10584-10588(1996).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 6-109.
RX PubMed=9135118; DOI=10.1006/jmbi.1997.0922;
RA Steinbacher S., Miller S., Baxa U., Budisa N., Weintraub A., Seckler R.,
RA Huber R.;
RT "Phage P22 tailspike protein: crystal structure of the head-binding domain
RT at 2.3 A, fully refined structure of the endorhamnosidase at 1.56-A
RT resolution, and the molecular basis of O-antigen recognition and
RT cleavage.";
RL J. Mol. Biol. 267:865-880(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 114-667.
RX PubMed=10543960; DOI=10.1006/jmbi.1999.3165;
RA Baxa U., Steinbacher S., Weintraub A., Huber R., Seckler R.;
RT "Mutations improving the folding of phage P22 tailspike protein affect its
RT receptor binding activity.";
RL J. Mol. Biol. 293:693-701(1999).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 109-667.
RX PubMed=10737931;
RX DOI=10.1002/(sici)1097-0134(20000401)39:1<89::aid-prot10>3.0.co;2-q;
RA Schuler B., Furst F., Osterroth F., Steinbacher S., Huber R., Seckler R.;
RT "Plasticity and steric strain in a parallel beta-helix: rational mutations
RT in the P22 tailspike protein.";
RL Proteins 39:89-101(2000).
CC -!- FUNCTION: Structural component of the short non-contractile tail. The
CC tail comprises six spikes that mediate primary attachment to the host
CC cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic
CC activity, hydrolyzing the alpha-1,3-O-glycosidic 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 {ECO:0000269|PubMed:12837775, ECO:0000269|PubMed:20817910}.
CC -!- SUBUNIT: Homotrimer. Interacts with the host O-antigen
CC lipopolysaccharides; this interaction induces cleavage of host O-
CC antigen. {ECO:0000269|PubMed:20817910, ECO:0000269|PubMed:8855221}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- DOMAIN: The interdigitation of the polypeptide chains at the C-termini
CC is important to protrimer formation in the folding pathway and to
CC thermostability of the mature protein.
CC -!- SIMILARITY: Belongs to the P22likevirus tail fiber protein family.
CC {ECO:0000305}.
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DR EMBL; J02473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF217253; AAF75060.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA00981.1; -; Genomic_DNA.
DR PIR; A18750; TLBP22.
DR RefSeq; NP_059644.1; NC_002371.2.
DR PDB; 1CLW; X-ray; 2.00 A; A=114-667.
DR PDB; 1LKT; X-ray; 2.60 A; A/B/C/D/E/F=6-109.
DR PDB; 1QA1; X-ray; 2.00 A; A=114-667.
DR PDB; 1QA2; X-ray; 2.00 A; A=114-667.
DR PDB; 1QA3; X-ray; 2.00 A; A=114-667.
DR PDB; 1QQ1; X-ray; 1.80 A; A=109-667.
DR PDB; 1QRB; X-ray; 2.00 A; A=109-667.
DR PDB; 1QRC; X-ray; 2.50 A; A=109-667.
DR PDB; 1TSP; X-ray; 2.00 A; A=109-667.
DR PDB; 1TYU; X-ray; 1.80 A; A=114-667.
DR PDB; 1TYV; X-ray; 1.80 A; A=114-667.
DR PDB; 1TYW; X-ray; 1.80 A; A=114-667.
DR PDB; 1TYX; X-ray; 1.80 A; A=114-667.
DR PDB; 2VFM; X-ray; 1.50 A; A=110-667.
DR PDB; 2VFN; X-ray; 1.50 A; A=110-667.
DR PDB; 2VFO; X-ray; 1.50 A; A=110-667.
DR PDB; 2VFP; X-ray; 1.55 A; A=110-667.
DR PDB; 2VFQ; X-ray; 1.55 A; A=110-667.
DR PDB; 2VKY; X-ray; 2.05 A; B=2-124.
DR PDB; 2VNL; X-ray; 1.80 A; A=2-122.
DR PDB; 2XC1; X-ray; 1.65 A; A/B/C=2-667.
DR PDB; 3TH0; X-ray; 1.75 A; A=109-667.
DR PDB; 5GAI; EM; 10.50 A; 0/Y/Z=6-667.
DR PDBsum; 1CLW; -.
DR PDBsum; 1LKT; -.
DR PDBsum; 1QA1; -.
DR PDBsum; 1QA2; -.
DR PDBsum; 1QA3; -.
DR PDBsum; 1QQ1; -.
DR PDBsum; 1QRB; -.
DR PDBsum; 1QRC; -.
DR PDBsum; 1TSP; -.
DR PDBsum; 1TYU; -.
DR PDBsum; 1TYV; -.
DR PDBsum; 1TYW; -.
DR PDBsum; 1TYX; -.
DR PDBsum; 2VFM; -.
DR PDBsum; 2VFN; -.
DR PDBsum; 2VFO; -.
DR PDBsum; 2VFP; -.
DR PDBsum; 2VFQ; -.
DR PDBsum; 2VKY; -.
DR PDBsum; 2VNL; -.
DR PDBsum; 2XC1; -.
DR PDBsum; 3TH0; -.
DR PDBsum; 5GAI; -.
DR SMR; P12528; -.
DR DrugBank; DB02590; Abequose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB04028; Tyvelose.
DR CAZy; GH90; Glycoside Hydrolase Family 90.
DR UniLectin; P12528; -.
DR PRIDE; P12528; -.
DR GeneID; 1262799; -.
DR KEGG; vg:1262799; -.
DR EvolutionaryTrace; P12528; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; Genome.
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: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; 2.160.20.20; -; 1.
DR Gene3D; 2.170.14.10; -; 1.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR015331; P22_tailspike_C.
DR InterPro; IPR009093; P22_tailspike_N.
DR InterPro; IPR036730; P22_tailspike_N_sf.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF09008; Head_binding; 1.
DR Pfam; PF09251; PhageP22-tail; 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; 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..667
FT /note="Tail spike protein"
FT /id="PRO_0000077757"
FT ACT_SITE 360
FT /evidence="ECO:0000269|PubMed:8889178"
FT ACT_SITE 393
FT /evidence="ECO:0000269|PubMed:8889178"
FT ACT_SITE 396
FT /evidence="ECO:0000269|PubMed:8889178"
FT MUTAGEN 360
FT /note="E->Q: Complete loss of hydrolysis of O-antigen
FT oligosaccharides."
FT /evidence="ECO:0000269|PubMed:8889178"
FT MUTAGEN 393
FT /note="D->N: Complete loss of hydrolysis of O-antigen
FT oligosaccharides."
FT /evidence="ECO:0000269|PubMed:8889178"
FT MUTAGEN 396
FT /note="D->N: Complete loss of hydrolysis of O-antigen
FT oligosaccharides."
FT /evidence="ECO:0000269|PubMed:8889178"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2XC1"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 82..86
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2XC1"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2XC1"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2VFM"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:2VFO"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 167..170
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:2VFM"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2VFM"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:2VFM"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:2XC1"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:2VFM"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 277..287
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:2VFM"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 349..352
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:1TSP"
FT STRAND 381..389
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:2VFM"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 428..435
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 438..448
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 450..458
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 460..470
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 472..480
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 516..529
FT /evidence="ECO:0007829|PDB:2VFM"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 548..553
FT /evidence="ECO:0007829|PDB:2XC1"
FT STRAND 555..563
FT /evidence="ECO:0007829|PDB:2VFM"
FT TURN 566..568
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 570..572
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 574..581
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 590..598
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 601..610
FT /evidence="ECO:0007829|PDB:2VFM"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 616..618
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:2VFM"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 633..642
FT /evidence="ECO:0007829|PDB:2VFM"
FT TURN 643..646
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 647..653
FT /evidence="ECO:0007829|PDB:2VFM"
FT STRAND 659..665
FT /evidence="ECO:0007829|PDB:2VFM"
SQ SEQUENCE 667 AA; 71857 MW; D05076D2732A4F7C CRC64;
MTDITANVVV SNPRPIFTES RSFKAVANGK IYIGQIDTDP VNPANQIPVY IENEDGSHVQ
ITQPLIINAA GKIVYNGQLV KIVTVQGHSM AIYDANGSQV DYIANVLKYD PDQYSIEADK
KFKYSVKLSD YPTLQDAASA AVDGLLIDRD YNFYGGETVD FGGKVLTIEC KAKFIGDGNL
IFTKLGKGSR IAGVFMESTT TPWVIKPWTD DNQWLTDAAA VVATLKQSKT DGYQPTVSDY
VKFPGIETLL PPNAKGQNIT STLEIRECIG VEVHRASGLM AGFLFRGCHF CKMVDANNPS
GGKDGIITFE NLSGDWGKGN YVIGGRTSYG SVSSAQFLRN NGGFERDGGV IGFTSYRAGE
SGVKTWQGTV GSTTSRNYNL QFRDSVVIYP VWDGFDLGAD TDMNPELDRP GDYPITQYPL
HQLPLNHLID NLLVRGALGV GFGMDGKGMY VSNITVEDCA GSGAYLLTHE SVFTNIAIID
TNTKDFQANQ IYISGACRVN GLRLIGIRST DGQGLTIDAP NSTVSGITGM VDPSRINVAN
LAEEGLGNIR ANSFGYDSAA IKLRIHKLSK TLDSGALYSH INGGAGSGSA YTQLTAISGS
TPDAVSLKVN HKDCRGAEIP FVPDIASDDF IKDSSCFLPY WENNSTSLKA LVKKPNGELV
RLTLATL
