UniProtKB - Q9XJP3 (FIBER_BPSFV)

BLAST

>sp|Q9XJP3|FIBER_BPSFV Tail spike protein OS=Shigella phage Sf6 OX=10761 PE=1 SV=2
MTDIITNVVIGMPSQLFTMARSFKAVANGKIYIGKIDTDPVNPENQIQVYVENEDGSHVP
ASQPIVINAAGYPVYNGQIVKFVTEQGHSMAVYDAYGSQQFYFQNVLKYDPDQFGPDLIE
QLAQSGKYSQDNTKGDAMIGVKQPLPKAVLRTQHDKNKEAISILDFGVIDDGVTDNYQAI
QNAIDAVASLPSGGELFIPASNQAVGYIVGSTLLIPGGVNIRGVGKASQLRAKSGLTGSV
LRLSYDSDTIGRYLRNIRVTGNNTCNGIDTNITAEDSVIRQVYGWVFDNVMVNEVETAYL
MQGLWHSKFIACQAGTCRVGLHFLGQCVSVSVSSCHFSRGNYSADESFGIRIQPQTYAWS
SEAVRSEAIILDSETMCIGFKNAVYVHDCLDLHMEQLDLDYCGSTGVVIENVNGGFSFSN
SWIAADADGTEQFTGIYFRTPTSTQSHKIVSGVHINTANKNTAANNQSIAIEQSAIFVFV
SGCTLTGDEWAVNIVDINECVSFDKCIFNKPLRYLRSGGVSVTDCYLAGITEVQKPEGRY
NTYRGCSGVPSVNGIINVPVAVGATSGSAAIPNPGNLTYRVRSLFGDPASSGDKVSVSGV
TINVTRPSPVGVALPSMVEYLAI

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History
Entry version 73 (25 Oct 2017)
Sequence version 2 (30 May 2003)
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Protein

Tail spike protein

Gene

N/A

Organism

Shigella phage Sf6 (Shigella flexneri bacteriophage VI) (Bacteriophage SfVI)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Non-covalently bound to the neck of the phage capsid and mediating attachment of the viral particle to host cell-surface polysaccharide. It displays endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide.2 Publications1 Publication

pH dependenceⁱ

Optimum pH is 7.5.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	248	Substrate binding1 Publication	1
Siteⁱ	294	Substrate binding1 Publication	1
Active siteⁱ	367	Shared with dimeric partner1 Publication	1
Active siteⁱ	400	Shared with dimeric partner1 Publication	1

GO - Molecular functionⁱ

endo-1,3-alpha-L-rhamnosidase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 12424253

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

disruption by virus of host envelope lipopolysaccharide during virus entry Source: UniProtKB-KW
entry into host via enzymatic degradation of host anatomical structure
Source: UniProtKB
Inferred from direct assayⁱ
- 6284
metabolic process Source: UniProtKB-KW
pathogenesis Source: InterPro
virion attachment to host cell
Source: UniProtKB
Inferred from direct assayⁱ
- 18462681

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Glycosidase, Hydrolase
Biological process	Degradation of host cell envelope components during virus entry, Degradation of host lipopolysaccharides during virus entry, Host-virus interaction, Viral attachment to host cell, Virus entry into host cell

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Tail spike proteinCurated Short name: TSP Alternative name(s): Endo-1,3-alpha-L-rhamnosidaseCurated (EC:3.2.1.-3 Publications) EndorhamnosidaseCurated
Organismⁱ	Shigella phage Sf6 (Shigella flexneri bacteriophage VI) (Bacteriophage SfVI)
Taxonomic identifierⁱ	10761 [NCBI]
Taxonomic lineageⁱ	Viruses › dsDNA viruses, no RNA stage › Caudovirales › Podoviridae › P22virus
Virus hostⁱ	Shigella flexneri [TaxID: 623]

Subcellular locationⁱ

Virion
1 Publication
Manual assertion based on experiment inⁱ
- Ref.3
  "Enzymic and molecular properties of base-plate parts of bacteriophage P22."
  Iwashita S., Kanegasaki S.
  Eur. J. Biochem. 65:87-94(1976) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION, SUBCELLULAR LOCATION.

GO - Cellular componentⁱ

virus tail, fiber
Source: UniProtKB
Inferred from direct assayⁱ
- 18462681

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Viral tail fiber protein, Viral tail protein, Virion

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	248	D → N: 98.5% loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	294	E → Q: 87% loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	367	E → Q: Almost complete loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	400	D → N: Almost complete loss of enzymatic activity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000077758	1 – 623	Tail spike proteinAdd BLAST		623

Interactionⁱ

Subunit structureⁱ

Homotrimer.2 Publications

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-29798N

DIPⁱ

DIP-29798N

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	114 – 123	Combined sources	10
Helixⁱ	126 – 128	Combined sources	3
Helixⁱ	135 – 138	Combined sources	4
Beta strandⁱ	139 – 141	Combined sources	3
Helixⁱ	153 – 157	Combined sources	5
Helixⁱ	163 – 166	Combined sources	4
Beta strandⁱ	171 – 174	Combined sources	4
Helixⁱ	177 – 188	Combined sources	12
Beta strandⁱ	194 – 197	Combined sources	4
Beta strandⁱ	207 – 211	Combined sources	5
Beta strandⁱ	213 – 215	Combined sources	3
Beta strandⁱ	219 – 222	Combined sources	4
Beta strandⁱ	228 – 232	Combined sources	5
Beta strandⁱ	238 – 243	Combined sources	6
Beta strandⁱ	252 – 256	Combined sources	5
Beta strandⁱ	258 – 260	Combined sources	3
Beta strandⁱ	263 – 271	Combined sources	9
Beta strandⁱ	282 – 289	Combined sources	8
Beta strandⁱ	291 – 311	Combined sources	21
Beta strandⁱ	313 – 325	Combined sources	13
Beta strandⁱ	328 – 334	Combined sources	7
Beta strandⁱ	336 – 338	Combined sources	3
Beta strandⁱ	348 – 353	Combined sources	6
Turnⁱ	358 – 360	Combined sources	3
Beta strandⁱ	367 – 379	Combined sources	13
Beta strandⁱ	381 – 387	Combined sources	7
Beta strandⁱ	390 – 410	Combined sources	21
Beta strandⁱ	413 – 425	Combined sources	13
Beta strandⁱ	434 – 438	Combined sources	5
Beta strandⁱ	448 – 456	Combined sources	9
Beta strandⁱ	467 – 471	Combined sources	5
Beta strandⁱ	478 – 482	Combined sources	5
Beta strandⁱ	487 – 489	Combined sources	3
Beta strandⁱ	491 – 496	Combined sources	6
Beta strandⁱ	501 – 505	Combined sources	5
Beta strandⁱ	507 – 510	Combined sources	4
Beta strandⁱ	512 – 516	Combined sources	5
Beta strandⁱ	520 – 524	Combined sources	5
Beta strandⁱ	526 – 528	Combined sources	3
Beta strandⁱ	530 – 534	Combined sources	5
Beta strandⁱ	542 – 545	Combined sources	4
Beta strandⁱ	547 – 550	Combined sources	4
Beta strandⁱ	553 – 558	Combined sources	6
Beta strandⁱ	565 – 570	Combined sources	6
Beta strandⁱ	579 – 583	Combined sources	5
Helixⁱ	588 – 590	Combined sources	3
Beta strandⁱ	594 – 598	Combined sources	5
Beta strandⁱ	601 – 605	Combined sources	5
Beta strandⁱ	616 – 622	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9XJP3
SMRⁱ	Q9XJP3
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9XJP3

EvolutionaryTraceⁱ

Q9XJP3

Family & Domainsⁱ

Domainⁱ

The active site involves residues located on two different subunits.1 Publication

Sequence similaritiesⁱ

Belongs to the P22likevirus tail fiber protein family.Curated

Family and domain databases

Gene3Dⁱ	2.160.20.10, 1 hit 2.170.14.10, 1 hit
InterProⁱ	View protein in InterPro IPR009093 P22_tailspike_N IPR036730 P22_tailspike_N_sf IPR024535 Pectate_lyase_SF_prot IPR012334 Pectin_lyas_fold IPR011050 Pectin_lyase_fold/virulence
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF09008 Head_binding, 1 hit PF12708 Pectate_lyase_3, 1 hit
SUPFAMⁱ	SSF51126 SSF51126, 1 hit SSF51327 SSF51327, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q9XJP3-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTDIITNVVI GMPSQLFTMA RSFKAVANGK IYIGKIDTDP VNPENQIQVY 
        60         70         80         90        100
VENEDGSHVP ASQPIVINAA GYPVYNGQIV KFVTEQGHSM AVYDAYGSQQ 
       110        120        130        140        150
FYFQNVLKYD PDQFGPDLIE QLAQSGKYSQ DNTKGDAMIG VKQPLPKAVL 
       160        170        180        190        200
RTQHDKNKEA ISILDFGVID DGVTDNYQAI QNAIDAVASL PSGGELFIPA 
       210        220        230        240        250
SNQAVGYIVG STLLIPGGVN IRGVGKASQL RAKSGLTGSV LRLSYDSDTI 
       260        270        280        290        300
GRYLRNIRVT GNNTCNGIDT NITAEDSVIR QVYGWVFDNV MVNEVETAYL 
       310        320        330        340        350
MQGLWHSKFI ACQAGTCRVG LHFLGQCVSV SVSSCHFSRG NYSADESFGI 
       360        370        380        390        400
RIQPQTYAWS SEAVRSEAII LDSETMCIGF KNAVYVHDCL DLHMEQLDLD 
       410        420        430        440        450
YCGSTGVVIE NVNGGFSFSN SWIAADADGT EQFTGIYFRT PTSTQSHKIV 
       460        470        480        490        500
SGVHINTANK NTAANNQSIA IEQSAIFVFV SGCTLTGDEW AVNIVDINEC 
       510        520        530        540        550
VSFDKCIFNK PLRYLRSGGV SVTDCYLAGI TEVQKPEGRY NTYRGCSGVP 
       560        570        580        590        600
SVNGIINVPV AVGATSGSAA IPNPGNLTYR VRSLFGDPAS SGDKVSVSGV 
       610        620 
TINVTRPSPV GVALPSMVEY LAI

Length:623

Mass (Da):67,066

Last modified:May 30, 2003 - v2

Checksum:ⁱ481FA9C23C349A9B

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF128887 Genomic DNA Translation: AAD33394.2

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

AF128887 Genomic DNA Translation: AAD33394.2

Protein	Similar proteins		Species	Score	Length	Source
Q9XJP3	Tail spike protein (Fragment)		SHIFL		342	UniRef100_Q9XJP3
UPI000181CFEE		BPSFV		514

Protein	Similar proteins		Species	Score	Length	Source
Q9XJP3	Tail spike protein (Fragment)		SHIFL		342	UniRef90_Q9XJP3
Gene 14 protein		BPSFV		623
UPI000775125B		ECOLX		623
UPI000181CFEE		BPSFV		514
UPI000E2E4B82		ECOLX		623
+4

Protein	Similar proteins		Species	Score	Length	Source
Q9XJP3	Tail spike protein (Fragment)		SHIFL		342	UniRef50_Q9XJP3
Gene 14 protein		BPSFV		623
UPI000775125B		ECOLX		623
UPI000181CFEE		BPSFV		514
UPI000E2E4B82		ECOLX		623
+4

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF128887 Genomic DNA Translation: AAD33394.2

Select the link destinations:
EMBLⁱ
GenBankⁱ
DDBJⁱ

Links Updated

AF128887 Genomic DNA Translation: AAD33394.2

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2VBE	X-ray	1.98	A	110-623	[»]
	2VBK	X-ray	1.25	A	110-623	[»]
	2VBM	X-ray	2.00	A	110-623	[»]
	4URR	X-ray	1.95	A/B/C/D/E/F	110-623	[»]
ProteinModelPortalⁱ	Q9XJP3
SMRⁱ	Q9XJP3
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

DIPⁱ	DIP-29798N

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9XJP3

EvolutionaryTraceⁱ

Q9XJP3

Family and domain databases

Gene3Dⁱ	2.160.20.10, 1 hit 2.170.14.10, 1 hit
InterProⁱ	View protein in InterPro IPR009093 P22_tailspike_N IPR036730 P22_tailspike_N_sf IPR024535 Pectate_lyase_SF_prot IPR012334 Pectin_lyas_fold IPR011050 Pectin_lyase_fold/virulence
Pfamⁱ	View protein in Pfam PF09008 Head_binding, 1 hit PF12708 Pectate_lyase_3, 1 hit
SUPFAMⁱ	SSF51126 SSF51126, 1 hit SSF51327 SSF51327, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	FIBER_BPSFV
Accessionⁱ	Q9XJP3Primary (citable) accession number: Q9XJP3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
	Last sequence update:	May 30, 2003
	Last modified:	October 25, 2017
	This is version 73 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Viral Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure

Documents

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

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9XJP3 (FIBER_BPSFV)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Tail spike protein

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Family and domain databases

Sequence databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

pH dependenceⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ