Phage RBP Database

Genbank accession

ANM45190.1 [GenBank]

Protein name

tail spike protein

RBP type

TSP

Evidence DepoScope

Probability 1,00

TF

Evidence GenBank

Probability 1,00

TSP

Evidence Phold

Probability 1,00

TSP

Evidence RBPdetect

Probability 0,91

TSP

Evidence RBPdetect2

Probability 0,98

TSP

Evidence UniProt/Swiss

Probability 1,00

TSP

Evidence UniProt/TrEMBL

Probability 1,00

Seq2Symm

C3 confidence 0,997

C3	0,997
C1	0,559
C2	0,004

Predicted homo-oligomer symmetry (Seq2Symm, per-class probabilities; C1 = monomer, C2 = dimer, C3 = trimer).

Protein sequence

MTDITANVVVSNPRPIFTESRSFKAVANGKIYIGQIDTDPVNPANQIPVYIENEDGSHVQITQPLIINAAGKIVYNGQLVKIVTVQGHSMAIYDANGSQVDYIANVLKYDPDQYSIEADKKFKYSVKLSDYPTLQDAASAAVDGLLIDRDYNFYGGETVDFGGKVLTIECKAKFIGDGNLIFTKLGKGSRIAGVFMESTTTPWVIKPWTDDNQWLTDAAAVVATLKQSKTDGYQPTVSDYVKFPGIETLLPPNAKGQNITSTLEIRECIGVEVHRASGLMAGFLFRGCHFCKMVDANNPSGGKDGIITFENLSGDWGKGNYVIGGRTSYGSVSSAQFLRNNGGFERDGGVIGFTSYRAGESGVKTWQGTVGSTTSRNYNLQFRDSVVIYPVWDGFDLGADTDMNPELDRPGDYPITQYPLHQLPLNHLIDNLLVRGALGVGFGMDGKGMYVSNITVEDCAGSGAYLLTHESVFTNIAIIDTNTKDFQANQIYISGACRVNGLRLIGIRSTDGQGLTIDAPNSTVSGITGMVDPSRINVANLAEEGLGNIRANSFGYDSAAIKLRIHKLSKTLDSGALYSHINGGAGSGSAYTQLTAISGSTPDAVSLKVNHKDCRGAEIPFVPDIASDDFIKDSSCFLPYWENNSTSLKALVKKPNGELVRLTLATL

Physico‐chemical properties

protein length:	667 AA
molecular weight:	71855,98720 Da
isoelectric point:	5,33857
aromaticity:	0,08846
hydropathy:	-0,16432

Domain architecture

ANM45190.1

1 667 aa

ATT 1–113 · STR 114–667

ATT Attachment Domain STR Structural Domain RBD Receptor-Binding Domain CBM Carbohydrate-Binding Module LEC Lectin-like Domain ENZ Enzymatic Domain CHP Intramolecular Chaperone LNK Linker/Spacer Domain TAS Tail-Associated Structural TTP Tail Tubular Protein UNK Uncharacterized Domain Unmapped

InterPro domains

IPR009093
ATT

IPR009093 IPR011050

IPR009093
ATT

IPR009093 IPR012332

IPR036730
ATT

IPR036730 G3DSA:2.160.20.20:FF:000002

G3DSA:2.170.14.10:FF:000001
Unmapped

G3DSA:2.170.14.10:FF:000001 IPR012332

IPR036730
ATT

IPR036730 IPR015331

ANM45190.1

1667 aa

ATT Attachment Domain STR Structural Domain RBD Receptor-Binding Domain CBM Carbohydrate-Binding Module LEC Lectin-like Domain ENZ Enzymatic Domain CHP Intramolecular Chaperone LNK Linker/Spacer Domain TAS Tail-Associated Structural TTP Tail Tubular Protein UNK Uncharacterized Domain Unmapped

InterPro domain annotations

Domain ID	Category	Cluster	Start	End	Layer	Name	Pref Zone	Confidence	Evidence	Support
IPR009093	ATT	DC_0597	1	113	InterPro cluster	Bacteriophage P22 tailspike, N-terminal	N-terminal	Medium	Text match	110 proteins / 110 hits
IPR009093	ATT	DC_0597	1	100	InterPro cluster	Bacteriophage P22 tailspike, N-terminal	N-terminal	Medium	Text match	110 proteins / 110 hits
IPR036730	ATT	IPR036730	2	110	Merged direct domain	Phage P22 tailspike-like, N-terminal domain superfamily	N-terminal	Low	Positional only	43 proteins / 43 hits
G3DSA:2.170.14.10:FF:000001	Unmapped	-	2	110	FunFam	Tail spike protein	-	-	-	-
IPR036730	ATT	IPR036730	7	109	Merged direct domain	Phage P22 tailspike-like, N-terminal domain superfamily	N-terminal	Low	Positional only	43 proteins / 43 hits
IPR012332	STR	IPR012332	100	667	Merged direct domain	Autotransporter, pectate lyase C-like domain superfamily	Central	Low	Positional only	199 proteins / 199 hits
G3DSA:2.160.20.20:FF:000002	Unmapped	-	111	667	FunFam	Tail spike protein	-	-	-	-
IPR012332	STR	IPR012332	111	667	Merged direct domain	Autotransporter, pectate lyase C-like domain superfamily	Central	Low	Positional only	199 proteins / 199 hits
IPR011050	STR	IPR011050	114	667	Merged direct domain	Pectin lyase fold/virulence factor	Central	Low	Positional only	572 proteins / 572 hits
IPR015331	RBD	DC_0844	116	665	InterPro cluster	P22 tailspike C-terminal domain	Central	High	Text match	401 proteins / 403 hits

Proteins with similar domain architecture

Segmented into three structural domains: N-terminal, central, and C-terminal.

Domain layout

ANM45190.1

1 667 aa

Domain	Start	End	Length (AA)	Confidence
N-terminal	1	130	130	0,9594
Central domain	131	554	425	0,9864
C-terminal	555	667	112	0,8663

N-terminal Central domain C-terminal

View these domains on the 3D structure via the Color by → Tail spike option in the Tertiary structure section below.

Phage

Salmonella phage 146851_sal5 [NCBI] · taxon 1813774

Uroviricota Caudoviricetes Lederbergvirus Salmonella phage 146851_sal5

Host

Salmonella enterica [NCBI] · taxon 28901

Pseudomonadota Gammaproteobacteria Enterobacterales Enterobacteriaceae Salmonella Salmonella enterica

Genbank protein accession

ANM45190.1 [NCBI]

Genbank nucleotide accession

KU927491.1 [NCBI]

CDS location

range 40833 -> 42836
strand +

CDS

ATGACAGACATCACTGCAAACGTAGTTGTTTCTAACCCTCGTCCAATCTTCACTGAATCCCGTTCGTTTAAAGCTGTTGCTAATGGGAAAATTTACATTGGTCAGATTGATACCGATCCGGTTAATCCTGCCAATCAGATACCCGTATACATTGAAAATGAGGATGGCTCTCACGTCCAGATTACTCAGCCGCTAATTATCAACGCAGCCGGTAAAATCGTATACAACGGCCAACTGGTGAAAATTGTCACCGTTCAGGGTCATAGCATGGCTATCTATGATGCCAATGGTTCTCAGGTTGACTATATTGCTAACGTATTGAAGTACGATCCAGATCAATATTCAATAGAAGCTGATAAAAAATTTAAGTATTCAGTAAAATTATCAGATTATCCAACATTGCAGGATGCAGCATCTGCTGCGGTTGATGGCCTTCTTATCGATCGAGATTATAATTTTTATGGTGGAGAGACAGTTGATTTTGGCGGAAAGGTTCTGACTATAGAATGTAAAGCTAAATTTATAGGAGATGGAAATCTTATTTTTACGAAATTAGGCAAAGGTTCCCGCATTGCCGGGGTTTTTATGGAAAGCACTACAACACCATGGGTTATCAAGCCTTGGACGGATGACAATCAGTGGCTAACGGATGCCGCAGCGGTCGTTGCCACTTTAAAACAATCTAAAACTGATGGGTATCAGCCAACCGTAAGCGATTACGTTAAATTCCCAGGAATAGAAACGTTACTCCCACCTAATGCAAAAGGGCAAAACATAACGTCTACGTTAGAAATTAGAGAATGTATAGGGGTCGAAGTTCATCGGGCTAGCGGTCTAATGGCTGGTTTTTTGTTTAGAGGGTGTCACTTCTGCAAGATGGTAGACGCCAATAATCCAAGCGGAGGTAAAGATGGCATTATAACCTTCGAAAACCTTAGCGGCGATTGGGGGAAGGGTAACTATGTCATTGGCGGACGAACCAGCTATGGGTCAGTAAGTAGCGCCCAGTTTTTACGTAATAATGGTGGCTTTGAACGTGATGGTGGAGTTATTGGGTTTACTTCATATCGCGCTGGGGAGAGTGGCGTTAAAACTTGGCAAGGTACTGTGGGCTCGACAACCTCTCGCAACTATAATCTGCAATTCCGCGACTCGGTCGTTATTTACCCCGTATGGGACGGATTCGATTTAGGTGCTGACACTGACATGAATCCGGAGTTGGACAGGCCAGGGGACTACCCTATAACCCAATACCCACTGCATCAGTTACCCCTAAATCACCTGATTGATAATCTTCTGGTTCGCGGGGCGTTAGGTGTAGGTTTTGGTATGGATGGTAAGGGCATGTATGTGTCTAATATTACCGTAGAAGATTGCGCTGGGTCTGGCGCGTACCTACTCACCCACGAATCAGTATTTACCAATATAGCCATAATTGACACCAATACTAAGGATTTCCAGGCGAATCAGATTTATATATCTGGGGCTTGCCGTGTGAACGGTTTACGTTTAATTGGGATCCGCTCAACCGATGGGCAGGGTCTAACCATAGACGCCCCTAACTCTACCGTAAGCGGTATAACCGGGATGGTAGACCCCTCTAGAATTAATGTTGCTAATTTGGCAGAAGAAGGGTTAGGTAATATCCGCGCTAATAGTTTCGGCTATGATAGCGCAGCGATTAAACTGCGGATTCATAAGTTATCAAAGACATTAGATAGCGGAGCATTGTACTCCCACATTAACGGGGGGGCCGGTTCTGGCTCAGCGTATACTCAACTTACTGCTATTTCAGGTAGCACACCTGACGCTGTATCATTAAAAGTTAACCACAAAGATTGCAGGGGGGCAGAGATACCATTTGTTCCTGACATCGCGTCAGATGATTTTATAAAGGATTCCTCATGTTTTTTGCCATATTGGGAAAATAATTCTACTTCTTTAAAGGCTTTAGTGAAAAAACCCAATGGAGAATTAGTTAGATTAACCTTGGCAACACTTTAG

A wet-lab result is recorded for this protein, or for its sequence: a solved structure, an experimental GO annotation, a UniProt ECO:0000269 assertion, or a GenBank /experiment= qualifier.

Tier	Source	Assay	Claim	Reference
Experimentally validated	PDB 8U10	structure:EM	—	ECO:0000006
Experimentally validated	PDB 5GAI	structure:EM	—	ECO:0000006
Experimentally validated	PDB 8EAN	structure:EM	—	ECO:0000006
Experimentally validated	PDB 8EB7	structure:EM	—	ECO:0000006
Experimentally validated	PDB 8TVR	structure:EM	—	ECO:0000006
Experimentally validated	PDB 8U11	structure:EM	—	ECO:0000006
Experimentally validated	PDB 8U1O	structure:EM	—	ECO:0000006
Experimentally validated	PDB 1LKT	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 3TH0	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 2XC1	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 2VNL	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 2VKY	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 2VFP	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1CLW	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1QA1	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1QA2	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1QA3	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1QQ1	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1QRB	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1QRC	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1TSP	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1TYV	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1TYW	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1TYX	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 2VFM	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 2VFN	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 2VFO	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 2VFQ	structure:X-ray	—	ECO:0000006
Experimentally validated	PDB 1TYU	structure:X-ray	—	ECO:0000006
Validated by sequence identity	GO GO:0098024	GO:IDA RBP	virus tail, fiber	ECO:0000314
Validated by sequence identity	GO GO:0052775	GO:IDA RBP	endo-1,3-alpha-L-rhamnosidase activity	ECO:0000314
Validated by sequence identity	GO GO:0044409	GO:IDA RBP	symbiont entry into host	ECO:0000314
Validated by sequence identity	GO GO:0019062	GO:IDA RBP	virion attachment to host cell	ECO:0000314
Validated by sequence identity	GenBank DAA00981.1	experiment:unspecified	tailspike protein – experimental evidence, no additional details recorded	—
Validated by sequence identity	GenBank NP_059644.1	experiment:unspecified	tail spike protein – experimental evidence, no additional details recorded	—
Validated by sequence identity	UniProt P12528	ECO:0000269:FUNCTION:12837775 RBP	Structural component of the short non-contractile tail (PubMed:37952769). The tail comprises six spikes that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane	PMID 12837775
Validated by sequence identity	UniProt P12528	ECO:0000269:FUNCTION:20817910 RBP	Structural component of the short non-contractile tail (PubMed:37952769). The tail comprises six spikes that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane	PMID 20817910
Validated by sequence identity	UniProt P12528	ECO:0000269:FUNCTION:37952769 RBP	Structural component of the short non-contractile tail (PubMed:37952769). The tail comprises six spikes that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane	PMID 37952769
Validated by sequence identity	UniProt P12528	ECO:0000269:SUBUNIT:20817910 RBP	Homotrimer (PubMed:8855221, PubMed:9135118). Interacts with the host O-antigen lipopolysaccharides; this interaction induces cleavage of host O-antigen (PubMed:20817910, PubMed:8855221). Interacts with tail hub protein gp10; this interaction anchors 6 fibers onto the tail hub hexamer (PubMed:37952769)	PMID 20817910
Validated by sequence identity	UniProt P12528	ECO:0000269:SUBUNIT:37952769 RBP	Homotrimer (PubMed:8855221, PubMed:9135118). Interacts with the host O-antigen lipopolysaccharides; this interaction induces cleavage of host O-antigen (PubMed:20817910, PubMed:8855221). Interacts with tail hub protein gp10; this interaction anchors 6 fibers onto the tail hub hexamer (PubMed:37952769)	PMID 37952769
Validated by sequence identity	UniProt P12528	ECO:0000269:SUBUNIT:8855221 RBP	Homotrimer (PubMed:8855221, PubMed:9135118). Interacts with the host O-antigen lipopolysaccharides; this interaction induces cleavage of host O-antigen (PubMed:20817910, PubMed:8855221). Interacts with tail hub protein gp10; this interaction anchors 6 fibers onto the tail hub hexamer (PubMed:37952769)	PMID 8855221
Validated by sequence identity	UniProt P12528	ECO:0000269:SUBUNIT:9135118 RBP	Homotrimer (PubMed:8855221, PubMed:9135118). Interacts with the host O-antigen lipopolysaccharides; this interaction induces cleavage of host O-antigen (PubMed:20817910, PubMed:8855221). Interacts with tail hub protein gp10; this interaction anchors 6 fibers onto the tail hub hexamer (PubMed:37952769)	PMID 9135118
Validated by sequence identity	UniProt P12528	protein_existence:evidence_at_protein_level	1: Evidence at protein level	—

Rows marked “Validated by sequence identity” come from a different entry carrying the same sequence — the experiment was not performed on this protein.

Title	Authors	Date	PMID	Source
Complete Genome Sequences of eight Podoviridae Bacteriophages infecting several subspecies of Salmonella enterica	Paradiso,R., Riccardi,M.G., Orsini,M., Galiero,G. and Borriello,G.	2016-12-29	—	GenBank

Protein

Domains

Tail Spike Domain Segmentation

Taxonomy

Coding sequence (CDS)

Genome Context

Tertiary structure

Predicted Aligned Error (PAE)

Experimental validation

Literature