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Protein

Tail spike protein

Gene
N/A
Organism
Enterobacteria phage K1F (Bacteriophage K1F)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tail spike protein: Responsible for initial absorption of the phage to the host bacterium. Degrades the alpha-2,8-linked polysialic acid K1 capsule by cleaving within the polymer chain of polysialic acid.2 Publications
C-terminal chaperone protein: The C-terminal chaperone protein mediates homotrimerization and proper folding of the catalytic endo-N trimer.1 Publication

Catalytic activityi

Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.3 Publications

Kineticsi

  1. KM=71 µM for poly-alpha-2,8-sialosyl carbohydrates1 Publication
  2. KM=1.2 mM for oligo-alpha-2,8-sialosyl carbohydrates1 Publication
  3. KM=7.1 µM for poly-alpha-2,8-alpha-2,9-sialosyl carbohydrates1 Publication
  1. Vmax=19 µmol/min/mg enzyme for poly-alpha-2,8-sialosyl carbohydrates cleavage1 Publication
  2. Vmax=18 µmol/min/mg enzyme for oligo-alpha-2,8-sialosyl carbohydrates cleavage1 Publication
  3. Vmax=13 µmol/min/mg enzyme for poly-alpha-2,8-alpha-2,9-sialosyl carbohydrates1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei542Binding to sialic acid1 Publication1
Sitei545Binding to sialic acid1 Publication1
Sitei549Binding to sialic acid1 Publication1
Sitei578Binding to sialic acid1 Publication1
Active sitei5812 Publications1
Active sitei5961 Publication1
Sitei598Binding to sialic acid1 Publication1
Sitei599Binding to sialic acid1 Publication1
Active sitei6472 Publications1

GO - Molecular functioni

  • endo-alpha-(2,8)-sialidase activity Source: UniProtKB

GO - Biological processi

  • entry into host via enzymatic degradation of host anatomical structure Source: UniProtKB
  • metabolic process Source: UniProtKB-KW
  • viral entry into host cell Source: UniProtKB-KW
  • virion attachment to host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Degradation of host capsule during virus entry, Degradation of host cell envelope components during virus entry, Host-virus interaction, Viral attachment to host adhesion receptor, Viral attachment to host cell, Virus entry into host cell

Enzyme and pathway databases

BRENDAi3.2.1.129. 716.

Protein family/group databases

CAZyiGH58. Glycoside Hydrolase Family 58.
MEROPSiS74.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Tail spike proteinCurated
Short name:
TSP
Alternative name(s):
Endo-N-acetylneuraminidase (EC:3.2.1.1293 Publications)
Short name:
Endo-N
Endo-alpha-sialidaseCurated
EndoNF
G102
Cleaved into the following chain:
OrganismiEnterobacteria phage K1F (Bacteriophage K1F)
Taxonomic identifieri344021 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesPodoviridaeAutographivirinaeT7likevirus
Virus hostiEscherichia coli [TaxID: 562]
Proteomesi
  • UP000001530 Componenti: Genome
  • UP000001722 Componenti: Genome

Subcellular locationi

Tail spike protein :
  • Virion

  • Note: Tail spike.1 Publication

GO - Cellular componenti

  • virus tail, fiber Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Viral tail fiber protein, Viral tail protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi328W → R: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi350H → A, N or Q: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi410K → A: 80% loss of enzymatic activity. 1 Publication1
Mutagenesisi542H → A: 60% loss of enzymatic activity. 1 Publication1
Mutagenesisi549R → A: Almost complete loss of enzymatic activity. 1 Publication1
Mutagenesisi581E → A: Almost complete loss of enzymatic activity. 2 Publications1
Mutagenesisi596R → A: Complete loss of enzymatic activity; when associated with A-581. Complete loss of enzymatic activity; when associated with A-647. 1 Publication1
Mutagenesisi647R → A: Almost complete loss of enzymatic activity. 2 Publications1
Mutagenesisi911S → A: Complete loss of proteolytic processing. 190-fold reduced enzymatic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by host1 Publication
ChainiPRO_00000577092 – 1064Tail spike proteinAdd BLAST1063
ChainiPRO_0000438182912 – 1064C-terminal chaperone protein1 PublicationAdd BLAST153

Post-translational modificationi

Proteolytic cleavage and release of the chaperone stabilizes the folded protein.2 Publications

Interactioni

Subunit structurei

Tail spike protein: Homotrimer (PubMed:3546309, PubMed:20124697). Interacts with sialic acid (PubMed:15608653, PubMed:20096705).4 Publications

Structurei

Secondary structure

11064
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi249 – 253Combined sources5
Helixi255 – 264Combined sources10
Beta strandi277 – 279Combined sources3
Helixi286 – 288Combined sources3
Beta strandi289 – 291Combined sources3
Beta strandi293 – 296Combined sources4
Beta strandi304 – 307Combined sources4
Beta strandi311 – 318Combined sources8
Beta strandi323 – 327Combined sources5
Beta strandi334 – 336Combined sources3
Beta strandi339 – 352Combined sources14
Beta strandi356 – 364Combined sources9
Beta strandi373 – 376Combined sources4
Turni380 – 384Combined sources5
Beta strandi385 – 388Combined sources4
Beta strandi392 – 395Combined sources4
Beta strandi398 – 407Combined sources10
Turni408 – 410Combined sources3
Beta strandi413 – 422Combined sources10
Beta strandi426 – 431Combined sources6
Beta strandi433 – 435Combined sources3
Beta strandi441 – 445Combined sources5
Beta strandi456 – 461Combined sources6
Beta strandi469 – 472Combined sources4
Beta strandi475 – 478Combined sources4
Beta strandi481 – 485Combined sources5
Beta strandi500 – 505Combined sources6
Beta strandi513 – 516Combined sources4
Beta strandi524 – 531Combined sources8
Beta strandi533 – 535Combined sources3
Beta strandi537 – 543Combined sources7
Beta strandi545 – 548Combined sources4
Beta strandi550 – 556Combined sources7
Turni557 – 561Combined sources5
Beta strandi567 – 570Combined sources4
Helixi573 – 575Combined sources3
Beta strandi579 – 587Combined sources9
Beta strandi590 – 598Combined sources9
Beta strandi606 – 612Combined sources7
Beta strandi618 – 621Combined sources4
Beta strandi633 – 636Combined sources4
Beta strandi639 – 645Combined sources7
Beta strandi667 – 674Combined sources8
Turni675 – 677Combined sources3
Beta strandi686 – 690Combined sources5
Beta strandi696 – 698Combined sources3
Beta strandi702 – 710Combined sources9
Beta strandi713 – 721Combined sources9
Turni728 – 734Combined sources7
Beta strandi746 – 753Combined sources8
Beta strandi772 – 774Combined sources3
Beta strandi784 – 786Combined sources3
Beta strandi790 – 792Combined sources3
Beta strandi796 – 803Combined sources8
Turni808 – 811Combined sources4
Beta strandi812 – 817Combined sources6
Beta strandi819 – 826Combined sources8
Helixi833 – 835Combined sources3
Beta strandi837 – 847Combined sources11
Helixi848 – 850Combined sources3
Beta strandi853 – 857Combined sources5
Beta strandi861 – 863Combined sources3
Beta strandi867 – 870Combined sources4
Beta strandi872 – 879Combined sources8
Beta strandi884 – 889Combined sources6
Beta strandi891 – 893Combined sources3
Beta strandi901 – 905Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V0EX-ray1.90A/B/C/D/E/F246-910[»]
1V0FX-ray2.55A/B/C/D/E/F246-910[»]
3GVJX-ray1.48A246-910[»]
3GVKX-ray1.84A/B/C246-910[»]
3GVLX-ray1.41A246-910[»]
3GW6X-ray2.60A/B/C/D/E/F790-913[»]
3JU4X-ray0.98A246-910[»]
ProteinModelPortaliQ04830.
SMRiQ04830.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04830.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati360 – 371BNR 1Add BLAST12
Repeati496 – 503BNR 28
Repeati608 – 619BNR 3Add BLAST12

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi198 – 216Gly-rich (hinge)Add BLAST19

Sequence similaritiesi

Belongs to the glycosyl hydrolase 58 family.Curated
Contains 3 BNR repeats.Curated

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di2.120.10.10. 2 hits.
2.40.30.20. 1 hit.
3.30.750.60. 1 hit.
4.10.1090.10. 1 hit.
InterProiIPR023366. ATP_synth_asu-like.
IPR024428. Endosialidase_beta_prop.
IPR024430. Endosialidase_C_dom.
IPR024429. Endosialidase_N-extension.
IPR001724. Glycl_Hydrolase_58.
IPR005604. Phage_T7_tail_fibre.
IPR030392. S74_ICA.
IPR011040. Sialidases.
[Graphical view]
PfamiPF12217. End_beta_propel. 1 hit.
PF12218. End_N_terminal. 1 hit.
PF12219. End_tail_spike. 1 hit.
PF13884. Peptidase_S74. 1 hit.
PF03906. Phage_T7_tail. 1 hit.
[Graphical view]
PRINTSiPR00849. GLHYDRLASE58.
SUPFAMiSSF50939. SSF50939. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q04830-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTITQFPSG NTQYRIEFDY LARTFVVVTL VNSSNPTLNR VLEVGRDYRF
60 70 80 90 100
LNPTMIEMLV DQSGFDIVRI HRQTGTDLVV DFRNGSVLTA SDLTTAELQA
110 120 130 140 150
IHIAEEGRDQ TVDLAKEYAD AAGSSAGNAK DSEDEARRIA ESIRAAGLIG
160 170 180 190 200
YMTRRSFEKG YNVTTWSEVL LWEEDGDYYR WDGTLPKNVP AGSTPETSGG
210 220 230 240 250
IGLGAWVSVG DAALRSQISN PEGAILYPEL HRARWLDEKD ARGWGAKGDG
260 270 280 290 300
VTDDTAALTS ALNDTPVGQK INGNGKTYKV TSLPDISRFI NTRFVYERIP
310 320 330 340 350
GQPLYYASEE FVQGELFKIT DTPYYNAWPQ DKAFVYENVI YAPYMGSDRH
360 370 380 390 400
GVSRLHVSWV KSGDDGQTWS TPEWLTDLHP DYPTVNYHCM SMGVCRNRLF
410 420 430 440 450
AMIETRTLAK NALTNCALWD RPMSRSLHLT GGITKAANQR YATIHVPDHG
460 470 480 490 500
LFVGDFVNFS NSAVTGVSGD MTVATVIDKD NFTVLTPNQQ TSDLNNAGKN
510 520 530 540 550
WHMGTSFHKS PWRKTDLGLI PSVTEVHSFA TIDNNGFAMG YHQGDVAPRE
560 570 580 590 600
VGLFYFPDAF NSPSNYVRRQ IPSEYEPDAS EPCIKYYDGV LYLITRGTRG
610 620 630 640 650
DRLGSSLHRS RDIGQTWESL RFPHNVHHTT LPFAKVGDDL IMFGSERAEN
660 670 680 690 700
EWEAGAPDDR YKASYPRTFY ARLNVNNWNA DDIEWVNITD QIYQGGIVNS
710 720 730 740 750
GVGVGSVVVK DNYIYYMFGG EDHFNPWTYG DNSAKDPFKS DGHPSDLYCY
760 770 780 790 800
KMKIGPDNRV SRDFRYGAVP NRAVPVFFDT NGVRTVPAPM EFTGDLGLGH
810 820 830 840 850
VTIRASTSSN IRSEVLMEGE YGFIGKSIPT DNPAGQRIIF CGGEGTSSTT
860 870 880 890 900
GAQITLYGAN NTDSRRIVYN GDEHLFQSAD VKPYNDNVTA LGGPSNRFTT
910 920 930 940 950
AYLGSNPIVT SNGERKTEPV VFDDAFLDAW GDVHYIMYQW LDAVQLKGND
960 970 980 990 1000
ARIHFGVIAQ QIRDVFIAHG LMDENSTNCR YAVLCYDKYP RMTDTVFSHN
1010 1020 1030 1040 1050
EIVEHTDEEG NVTTTEEPVY TEVVIHEEGE EWGVRPDGIF FAEAAYQRRK
1060
LERIEARLSA LEQK
Length:1,064
Mass (Da):118,905
Last modified:November 2, 2016 - v4
Checksum:i82FAB75EDC68DAB6
GO

Sequence cautioni

The sequence AAC37340 differs from that shown. Reason: Frameshift at position 914.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti628H → R in AAC37340 (PubMed:8331067).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63657 Unassigned DNA. Translation: AAC37340.1. Frameshift.
AJ505988 Genomic DNA. Translation: CAD44528.2.
DQ111067 Genomic DNA. Translation: AAZ73001.1.
AM084414 Genomic DNA. Translation: CAJ29390.1.
PIRiA36887.
RefSeqiYP_338127.1. NC_007456.1.

Genome annotation databases

GeneIDi3707741.
KEGGivg:3707741.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63657 Unassigned DNA. Translation: AAC37340.1. Frameshift.
AJ505988 Genomic DNA. Translation: CAD44528.2.
DQ111067 Genomic DNA. Translation: AAZ73001.1.
AM084414 Genomic DNA. Translation: CAJ29390.1.
PIRiA36887.
RefSeqiYP_338127.1. NC_007456.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V0EX-ray1.90A/B/C/D/E/F246-910[»]
1V0FX-ray2.55A/B/C/D/E/F246-910[»]
3GVJX-ray1.48A246-910[»]
3GVKX-ray1.84A/B/C246-910[»]
3GVLX-ray1.41A246-910[»]
3GW6X-ray2.60A/B/C/D/E/F790-913[»]
3JU4X-ray0.98A246-910[»]
ProteinModelPortaliQ04830.
SMRiQ04830.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH58. Glycoside Hydrolase Family 58.
MEROPSiS74.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi3707741.
KEGGivg:3707741.

Enzyme and pathway databases

BRENDAi3.2.1.129. 716.

Miscellaneous databases

EvolutionaryTraceiQ04830.

Family and domain databases

Gene3Di2.120.10.10. 2 hits.
2.40.30.20. 1 hit.
3.30.750.60. 1 hit.
4.10.1090.10. 1 hit.
InterProiIPR023366. ATP_synth_asu-like.
IPR024428. Endosialidase_beta_prop.
IPR024430. Endosialidase_C_dom.
IPR024429. Endosialidase_N-extension.
IPR001724. Glycl_Hydrolase_58.
IPR005604. Phage_T7_tail_fibre.
IPR030392. S74_ICA.
IPR011040. Sialidases.
[Graphical view]
PfamiPF12217. End_beta_propel. 1 hit.
PF12218. End_N_terminal. 1 hit.
PF12219. End_tail_spike. 1 hit.
PF13884. Peptidase_S74. 1 hit.
PF03906. Phage_T7_tail. 1 hit.
[Graphical view]
PRINTSiPR00849. GLHYDRLASE58.
SUPFAMiSSF50939. SSF50939. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiFIBER_BPK1F
AccessioniPrimary (citable) accession number: Q04830
Secondary accession number(s): Q2WC71, Q858B1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 2, 2016
Last modified: November 30, 2016
This is version 92 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.