FIBL1_BPT5
ID FIBL1_BPT5 Reviewed; 1396 AA.
AC P13390; O48502; Q5DMH0; Q66LT2;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 30-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Side tail fiber protein pb1 {ECO:0000305};
DE Short=STF-pb1 {ECO:0000305};
DE EC=3.4.21.-;
DE AltName: Full=Tail protein pb1 {ECO:0000303|PubMed:24198424};
DE Flags: Precursor;
GN Name=ltf {ECO:0000305};
GN ORFNames=T5.133, T5p131 {ECO:0000312|EMBL:AAU05270.1};
OS Escherichia phage T5 (Enterobacteria phage T5).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX NCBI_TaxID=2695836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7789514; DOI=10.1016/0014-5793(95)00482-o;
RA Kaliman A.V., Kulshin V.E., Shlyapnikov M.G., Ksenzenko V.N., Kryukov V.M.;
RT "The nucleotide sequence of the bacteriophage T5 ltf gene.";
RL FEBS Lett. 366:46-48(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT "Bacteriophage T5 complete genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 11303-B5 {ECO:0000312|EMBL:AAX12061.1};
RX PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA Hu S.;
RT "Complete genome sequence of bacteriophage T5.";
RL Virology 332:45-65(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11303-B5 {ECO:0000312|EMBL:CAJ29339.1};
RX PubMed=17158460; DOI=10.1074/jbc.m609543200;
RA Schwarzer D., Stummeyer K., Gerardy-Schahn R., Muehlenhoff M.;
RT "Characterization of a novel intramolecular chaperone domain conserved in
RT endosialidases and other bacteriophage tail spike and fiber proteins.";
RL J. Biol. Chem. 282:2821-2831(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SUBCELLULAR LOCATION,
RP FUNCTION, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=St0 deletion mutant;
RX PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA Boulanger P.;
RT "Insights into bacteriophage T5 structure from analysis of its
RT morphogenesis genes and protein components.";
RL J. Virol. 88:1162-1174(2014).
RN [6]
RP INTERACTION WITH HOST POLYMANNOSE O-ANTIGENS, AND FUNCTION.
RX PubMed=7045389; DOI=10.1128/jvi.41.1.222-227.1982;
RA Heller K., Braun V.;
RT "Polymannose O-antigens of Escherichia coli, the binding sites for the
RT reversible adsorption of bacteriophage T5+ via the L-shaped tail fibers.";
RL J. Virol. 41:222-227(1982).
RN [7]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE.
RX PubMed=3267228; DOI=10.1093/nar/16.13.6230;
RA Kaliman A.V., Kryukov V.M., Bayev A.A.;
RT "The nucleotide sequence of bacteriophage T5 DNA at the region between
RT early and late genes.";
RL Nucleic Acids Res. 16:6230-6230(1988).
RN [8] {ECO:0007744|PDB:4UW7, ECO:0007744|PDB:4UW8}
RP X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 970-1396, SUBUNIT, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=24316831; DOI=10.1107/s1744309113028959;
RA Garcia-Doval C., Luque D., Caston J.R., Boulanger P., van Raaij M.J.;
RT "Crystallization of the C-terminal domain of the bacteriophage T5 L-shaped
RT fibre.";
RL Acta Crystallogr. F 69:1363-1367(2013).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 970-1263, AND SUBUNIT.
RX PubMed=26670244; DOI=10.3390/v7122946;
RA Garcia-Doval C., Caston J.R., Luque D., Granell M., Otero J.M.,
RA Llamas-Saiz A.L., Renouard M., Boulanger P., van Raaij M.J.;
RT "Structure of the receptor-binding carboxy-terminal domain of the
RT bacteriophage T5 L-shaped tail fibre with and without its intra-molecular
RT chaperone.";
RL Viruses 7:6424-6440(2015).
CC -!- FUNCTION: Assembles together with p132 to form the three L-shaped long
CC tail fibers and the collar structure at the junction between the tail
CC tube and the conical tail tip (PubMed:24198424). The three L-shaped
CC long tail fibers recognize the host lipopolysaccharides that serve as
CC adhesion receptor for virus entry (PubMed:7045389). Each fiber consists
CC of a thin proximal rod of about 30 nm connected by a hinge to a thicker
CC distal part of about 47 nm (PubMed:24198424).
CC {ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:7045389}.
CC -!- SUBUNIT: Homotrimer (PubMed:24316831). Interacts with the O-antigens of
CC host lipopolysaccharides (PubMed:7045389).
CC {ECO:0000269|PubMed:24316831, ECO:0000269|PubMed:7045389}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:24198424}. Note=Part
CC of the tail long fibers. {ECO:0000269|PubMed:24198424}.
CC -!- PTM: The cleaved C-terminus functions as an intramolecular chaperone
CC and is removed by an autoproteolytic process after correct
CC trimerization and folding. {ECO:0000269|PubMed:24316831,
CC ECO:0000269|PubMed:26670244}.
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DR EMBL; AY543070; AAQ92751.2; -; Genomic_DNA.
DR EMBL; AY692264; AAU05270.1; -; Genomic_DNA.
DR EMBL; AY587007; AAX12061.1; -; Genomic_DNA.
DR EMBL; AM084272; CAJ29339.1; -; Genomic_DNA.
DR PIR; S01982; S01982.
DR PIR; S65934; S36851.
DR RefSeq; YP_006961.1; NC_005859.1.
DR PDB; 4UW7; X-ray; 2.52 A; A/B/C=970-1263.
DR PDB; 4UW8; X-ray; 2.52 A; A/B/C/D/E/F/G/H/I=970-1396.
DR PDB; 5AQ5; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=970-1263.
DR PDBsum; 4UW7; -.
DR PDBsum; 4UW8; -.
DR PDBsum; 5AQ5; -.
DR SMR; P13390; -.
DR GeneID; 2777639; -.
DR KEGG; vg:2777639; -.
DR Proteomes; UP000002107; Genome.
DR Proteomes; UP000002141; Genome.
DR Proteomes; UP000002503; Genome.
DR GO; GO:0098024; C:virus tail, fiber; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0039638; P:lipopolysaccharide-mediated virion attachment to host cell; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR030392; S74_ICA.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PROSITE; PS51688; ICA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Host-virus interaction; Hydrolase; Late protein;
KW Protease; Reference proteome; Serine protease;
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..1263
FT /note="Side tail fiber protein pb1"
FT /id="PRO_0000165221"
FT PROPEP 1264..1396
FT /note="Intramolecular chaperone"
FT /evidence="ECO:0000269|PubMed:24316831"
FT /id="PRO_0000435545"
FT DOMAIN 1264..1394
FT /note="Peptidase S74"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01025"
FT REGION 51..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 187..214
FT /evidence="ECO:0000255"
FT COILED 1263..1396
FT /evidence="ECO:0000269|PubMed:26670244"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1263..1264
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:24198424,
FT ECO:0000269|PubMed:24316831"
FT CONFLICT 42..43
FT /note="DV -> EL (in Ref. 5; AAU05270, 3; AAX12061 and 4;
FT CAJ29339)"
FT /evidence="ECO:0000305"
FT CONFLICT 54..55
FT /note="GP -> AA (in Ref. 5; AAU05270, 3; AAX12061 and 4;
FT CAJ29339)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155
FT /note="D -> E (in Ref. 5; AAU05270)"
FT /evidence="ECO:0000305"
FT STRAND 990..999
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1001..1007
FT /evidence="ECO:0007829|PDB:5AQ5"
FT HELIX 1010..1012
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1020..1027
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1031..1034
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1039..1048
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1057..1064
FT /evidence="ECO:0007829|PDB:5AQ5"
FT HELIX 1070..1072
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1074..1079
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1085..1087
FT /evidence="ECO:0007829|PDB:5AQ5"
FT TURN 1090..1092
FT /evidence="ECO:0007829|PDB:4UW7"
FT HELIX 1095..1097
FT /evidence="ECO:0007829|PDB:5AQ5"
FT HELIX 1103..1109
FT /evidence="ECO:0007829|PDB:5AQ5"
FT HELIX 1117..1119
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1122..1127
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1133..1139
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1148..1156
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1158..1162
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1173..1180
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1190..1199
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1208..1215
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1222..1228
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1234..1238
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1244..1246
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1254..1258
FT /evidence="ECO:0007829|PDB:5AQ5"
FT STRAND 1261..1263
FT /evidence="ECO:0007829|PDB:4UW8"
FT HELIX 1266..1268
FT /evidence="ECO:0007829|PDB:4UW8"
FT HELIX 1277..1287
FT /evidence="ECO:0007829|PDB:4UW8"
FT STRAND 1291..1293
FT /evidence="ECO:0007829|PDB:4UW8"
FT STRAND 1306..1309
FT /evidence="ECO:0007829|PDB:4UW8"
FT HELIX 1312..1321
FT /evidence="ECO:0007829|PDB:4UW8"
FT HELIX 1326..1328
FT /evidence="ECO:0007829|PDB:4UW8"
FT STRAND 1332..1337
FT /evidence="ECO:0007829|PDB:4UW8"
FT STRAND 1340..1346
FT /evidence="ECO:0007829|PDB:4UW8"
FT STRAND 1357..1362
FT /evidence="ECO:0007829|PDB:4UW8"
FT STRAND 1365..1370
FT /evidence="ECO:0007829|PDB:4UW8"
FT HELIX 1372..1393
FT /evidence="ECO:0007829|PDB:4UW8"
SQ SEQUENCE 1396 AA; 147962 MW; 9A804F651B272302 CRC64;
MAITKIILQQ MVTMDQNSIT ASKYPKYTVV LSNSISSITA ADVTSAIESS KASGPAAKQS
EINAKQSELN AKDSENEAEI SATSSQQSAT QSASSATASA NSAKAAKTSE TNANNSKNAA
KTSETNAASS ASSASSFATA AENSARAAKT SETNAGNSAQ AADASKTAAA NSATAAKTSE
TNAKKSETAA KTSETNAKTS ENKAKEYLDM ASELVSPVTQ YDWPVGTNNN SVYVKIAKLT
DPGAVSCHLT LMITNGGNYG SSYGNIDFVE ISARGLNDAR GVTSENITKF LSVRRLGSPN
LAWDNQLRYG LVEGDGYFEV WCYQRAFIKE TRVAVLAQTG RTELYIPEGF VSQDTQPSGF
IESLAARIYD QVNKPTKADL GLENAMLVGA FGLGGNGLSY SSVQSNVDLI NKLKANGGQY
WRAARESGAN VDINDHGSGF YSHCGDTHAA INVQYNTGIV KVLATTDRNL ASDIVYANTL
YGTANKPSKS DVGLGNVTND AQVKKAGDVM SGDLDIRKET PSIRLKSTQG NAHLWFMNND
GGERGVIWSP PNNGSLGEIH IRAKTSDGTS TGDFIVRHDG RIEAKDAKIS YKISSRTAEF
SNDDTNTAAT NLRVSGKQHT PIMLVRDSDS NVSVGFKLNN MNAKLLGIDI DGDLAFGENP
DHKQNSKIVT RKMMDAGFSV AGLMDFTNGF AGPWEAKNIS DQELDLNSLM IKKSDPGSIR
VYQCVSAGGG NNITNKPSGI GGNFILYVES IRKVGDTDFT NRQRLFGTDL NREFTRYCSN
GTWSAWRESV VSGMNQDVSV KSMSVSGRLS GNELSVGGAG VLNGNLGVGG GATSKMPSSD
KGIVIGRGSI VREGGEGRLI LSSSGGTDRL LQLRPAGATS LDNQVEISCT SASAGDTKIS
FGQGAAIRCN NAGSPIISAK AGQMIYFRPN GDGISEGQMI LSPNGDLVVK GGVNSKEIDV
TASQSLPLKE TTATTGIGVN FIGDSATECS FGIENTAGGS AVFHNYTRGA SNSVTKNNQL
LGGYGSRPWL GSTYTEHSNA ALHFLGAGDT SATNHGGWIR LLVTPKGKTI SDRVPAFRLS
DNGDLWLVPD GAMHSDLGLV RSIETLNAAV PRFNAPSIQD GRGLKIVAPQ APEIDLIAPR
GSGASAPAIR AMWCDGSLAD TTRYIGATQP GSTFYIGASG HDGEKFDSMR GSVAIKSAGG
WGPTSTPTQV VLETCESGSI SRLPRWGVDH NGTLMPMADN RYNLGWGSGR VKQVYAVNGT
INTSDARLKN DVRAMSDPET EAAKAIAKEI GFWTWKEQAD MNDIREHCGL TVQRAIEIME
SFGLDPFKYG FICYDKWDEH TVVSEYGPAN EDGTENPIYK TIPAGDHYSF RLEELNLFIA
KGFEARLSAI EDKLGM
