Protein

UniProt accession
Q9XJP3 [UniProt]
Protein name
Tail spike protein
RBP type
TSP
Evidence DepoScope
Probability 1,00
TSP
Evidence RBPdetect
Probability 0,91
TSP
Evidence RBPdetect2
Probability 0,95
Protein sequence
MTDIITNVVIGMPSQLFTMARSFKAVANGKIYIGKIDTDPVNPENQIQVYVENEDGSHVPASQPIVINAAGYPVYNGQIVKFVTEQGHSMAVYDAYGSQQFYFQNVLKYDPDQFGPDLIEQLAQSGKYSQDNTKGDAMIGVKQPLPKAVLRTQHDKNKEAISILDFGVIDDGVTDNYQAIQNAIDAVASLPSGGELFIPASNQAVGYIVGSTLLIPGGVNIRGVGKASQLRAKSGLTGSVLRLSYDSDTIGRYLRNIRVTGNNTCNGIDTNITAEDSVIRQVYGWVFDNVMVNEVETAYLMQGLWHSKFIACQAGTCRVGLHFLGQCVSVSVSSCHFSRGNYSADESFGIRIQPQTYAWSSEAVRSEAIILDSETMCIGFKNAVYVHDCLDLHMEQLDLDYCGSTGVVIENVNGGFSFSNSWIAADADGTEQFTGIYFRTPTSTQSHKIVSGVHINTANKNTAANNQSIAIEQSAIFVFVSGCTLTGDEWAVNIVDINECVSFDKCIFNKPLRYLRSGGVSVTDCYLAGITEVQKPEGRYNTYRGCSGVPSVNGIINVPVAVGATSGSAAIPNPGNLTYRVRSLFGDPASSGDKVSVSGVTINVTRPSPVGVALPSMVEYLAI
Physico‐chemical
properties
protein length:623 AA
molecular weight: 67065,69120 Da
isoelectric point:5,09513
aromaticity:0,08668
hydropathy:-0,03435

Domains

Taxonomy

  Name Taxonomy ID Lineage
Phage Shigella phage Sf6
[NCBI]
2905959 Viruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes
Host No host information

Coding sequence (CDS)

Coding sequence (CDS)

No CDS data available.

Gene Ontology

Description Category Evidence (source)
GO:0098024 virus tail, fiber Cellular Component IDA:UniProtKB (UniProt)
GO:0052775 endo-1,3-alpha-L-rhamnosidase activity Molecular Function IDA:UniProtKB (UniProt)
GO:0044409 symbiont entry into host Biological Process IDA:UniProtKB (UniProt)
GO:0098994 symbiont entry into host cell via disruption of host cell envelope Biological Process IEA:UniProtKB-KW (UniProt)
GO:0098995 symbiont entry into host cell via disruption of host cell envelope lipopolysaccharide Biological Process IEA:UniProtKB-KW (UniProt)
GO:0019062 virion attachment to host cell Biological Process IDA:UniProtKB (UniProt)

Enzymatic activity

No enzymatic activity data available.

Tertiary structure

PDB ID
2VBE
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
PDB ID
2VBK
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
PDB ID
2VBM
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
PDB ID
4URR
PDB
Source PDB
Method X-ray
Resolution 1,0000
Evidence 1,0000
PDB ID
7SG7
PDB
Source PDB
Method EM
Resolution 1,0000
Evidence 1,0000
PDB ID
7UKJ
PDB
Source PDB
Method EM
Resolution 1,0000
Evidence 1,0000
PDB ID
e65d0a8b910307962c0c4b66affe666068c94983828182a52e9b45343130689c
ESMFold
Source ESMFold
Method ESMFold
Resolution 0,8401
Evidence 0,8401

Literature

Title Authors Date PMID Source
Enzymic and molecular properties of base-plate parts of bacteriophage P22. Iwashita S, Kanegasaki S 1976-05-17 6284 PubMed
The tailspike protein of Shigella phage Sf6. A structural homolog of Salmonella phage P22 tailspike protein without sequence similarity in the beta-helix domain. Freiberg A, Morona R, Van den Bosch L, Jung C, Behlke J, Carlin N, Seckler R, Baxa U 2003-01-17 12424253 PubMed
An intersubunit active site between supercoiled parallel beta helices in the trimeric tailspike endorhamnosidase of Shigella flexneri Phage Sf6. Müller JJ, Barbirz S, Heinle K, Freiberg A, Seckler R, Heinemann U 2008-05 18462681 PubMed
Enzymic and Molecular Properties of Base-Plate Parts of Bacteriophage P22 Shintaro IWASHITA, Shiro KANEGASAKI 1976-05 10.1111/j.1432-1033.1976.tb10392.x DOI
The Shigella flexneri bacteriophage Sf6 tailspike protein (TSP)/endorhamnosidase is related to the bacteriophage P22 TSP and has a motif common to exo- and endoglycanases, and C-5 epimerases James E. H. Chua, Paul A. Manning, Renato Morona 1999-07-01 10.1099/13500872-145-7-1649 DOI
The Tailspike Protein of Shigella Phage Sf6 Alexander Freiberg, Renato Morona, Luisa Van Den Bosch, Christiane Jung, Joachim Behlke, Nils Carlin, Robert Seckler, Ulrich Baxa 2003-01 10.1074/jbc.m205294200 DOI
An Intersubunit Active Site between Supercoiled Parallel β Helices in the Trimeric Tailspike Endorhamnosidase of Shigella flexneri Phage Sf6 Jürgen J. Müller, Stefanie Barbirz, Karolin Heinle, Alexander Freiberg, Robert Seckler, Udo Heinemann 2008-05 10.1016/j.str.2008.01.019 DOI