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Entry version 73 (02 Jun 2021)
Sequence version 1 (01 Dec 2001)
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Protein

Platelet binding protein GspB

Gene

gspB

Organism
Streptococcus gordonii
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Plays a role in virulence and host-pathogen interactions. Mediates binding to human platelets via interaction with the human cell surface glycoprotein GP1BA (PubMed:21765814).

Plays a positive role in biofilm formation, possibly by self-association via the basic region (BR) (PubMed:20714350).

2 Publications

Miscellaneous

S.gordonii, a commensal oral cavity bacteria, is among the bacteria most frequently identified as being the primary etiological agents of subacute infective endocarditis (found in 13% of cases).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei443Important for interaction with host glycoprotein and virulence1
Sitei484Important for interaction with host glycoprotein and virulence1
Sitei485Important for interaction with host glycoprotein and virulence1

<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 - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion, Virulence

Protein family/group databases

UniLectin database of carbohydrate-binding proteins

More...
UniLectini
Q939N5

<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 subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Platelet binding protein GspB
Alternative name(s):
Adhesin GspBCurated
Serine-rich adhesin for platelets
Serine-rich repeat protein GspB
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:gspB
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiStreptococcus gordonii
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1302 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

<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

Keywords - Cellular componenti

Cell wall, Secreted

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Loss of adherence to human platelet cells (PubMed:12010500). Decrease in early biofilm formation (PubMed:20714350).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi443Y → F: Strongly reduced interaction with GP1BA carbohydrate chains. 1 Publication1
Mutagenesisi484R → E: Strongly reduced interaction with GP1BA carbohydrate chains. Strongly reduced platelet binding. 1 Publication1
Mutagenesisi485Y → F: Strongly reduced interaction with GP1BA carbohydrate chains. 1 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 85Sequence analysisAdd BLAST85
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000041419286 – 3041Platelet binding protein GspBAdd BLAST2956
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00004141933042 – 3072Removed by sortasePROSITE-ProRule annotationAdd BLAST31

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei3041Pentaglycyl murein peptidoglycan amidated threoninePROSITE-ProRule annotation1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Proteolytically cleaved by a metalloprotease.By similarity
Both SSR1 and SSR2 domains are glycosylated (Probable). A truncated derivative (residues 1-2062) contains 105 nmol per nmol of protein, suggesting at least 10% of the apparent molecular weight is due to carbohydrates (PubMed:14729688). Glucose and N-acetylglucosamine are present in a ratio of 30:73 residues per truncated polypeptide, as well as minor amounts of galactose and N-acetylgalactosamine (PubMed:14729688). Glycosylation occurs intracellularly in the Ser-rich regions SSR1 and SSR2 (PubMed:14729688, PubMed:15489421). Glycosylation of SSR2 domain may be required to prevent aggregation of GspB (Probable). It is probable that most of the Ser residues in SSR1 and SSR2 are O-GlcNAcylated. Sequential glycosylation by sugar transferases are able to generate complex sugar polymorphisms (By similarity).By similarity3 Publications2 Publications

Keywords - PTMi

Glycoprotein, Peptidoglycan-anchor

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Both SSR domains in the unglycosylated protein bind to Asp2 and Asp3; glycosylated protein binds less well.

Interacts with the human cell surface glycoprotein GP1BA.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
Q939N5, 2 interactors

<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

13072
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q939N5

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni117 – 147DisorderedSequence analysisAdd BLAST31
Regioni123 – 236Ser-rich region 1 (SSR1)Add BLAST114
Regioni182 – 254DisorderedSequence analysisAdd BLAST73
Regioni237 – 603Basic region (BR)Add BLAST367
Regioni604 – 3028Ser-rich region 2 (SSR2)Add BLAST2425
Regioni876 – 909DisorderedSequence analysisAdd BLAST34
Regioni936 – 969DisorderedSequence analysisAdd BLAST34
Regioni1024 – 2085DisorderedSequence analysisAdd BLAST1062
Regioni2106 – 2139DisorderedSequence analysisAdd BLAST34
Regioni2173 – 2223DisorderedSequence analysisAdd BLAST51
Regioni2250 – 2595DisorderedSequence analysisAdd BLAST346
Regioni2625 – 2967DisorderedSequence analysisAdd BLAST343
Regioni3014 – 3045DisorderedSequence analysisAdd BLAST32

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi3038 – 3042LPXTG sorting signalPROSITE-ProRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi182 – 237Polar residuesSequence analysisAdd BLAST56
Compositional biasi3014 – 3044Polar residuesSequence analysisAdd BLAST31

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Has a short and long Ser-rich region with a basic region between them. The SRR domains themselves are comprised of inexact repeats of SASESASTSASV. SSR1 has 6 repeats, SSR2 has 200. The Ser-rich regions are both glycosylated. The basic region (BR) binds to whole cell lysates of wild-type but not bacteria deleted of this gene; it also recognizes whole cell lysates of S.aureus strain ISP479C probably via SraP, but not lysates of S.pneumoniae TIGR4 (PubMed:20714350). The predicted pI of the basic region is 9.51 (PubMed:19202081).1 Publication1 Publication

<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

Keywords - Domaini

Signal

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR044024, aRib
IPR019948, Gram-positive_anchor
IPR022263, KxYKxGKxW
IPR019931, LPXTG_anchor
IPR026465, Ser_adhes_glycop

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18938, aRib, 1 hit
PF00746, Gram_pos_anchor, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03715, KxYKxGKxW, 1 hit
TIGR04224, ser_adhes_Nterm, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50847, GRAM_POS_ANCHORING, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q939N5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFFKRQKGQY HEVERVTRFK LIKSGKHWLR AATSQFGLLR LMKGSDVSST
60 70 80 90 100
EVKVVEEQSV EKSGLNYLKG IIATGAVLGG AVVTSSSVYA EEEQAHEKVI
110 120 130 140 150
DTRDVLATRG EAVLSEEAAT TLSSTEANPV ESLSDTLSAS ESTSASSSVS
160 170 180 190 200
TSISVSESFS VSGSLSYSTS LSQSVSASAS ASESLSVSSS ASDSVSASTS
210 220 230 240 250
TSASASQSVS ASQKSTISTS ESTRSESSQQ STEASSQTGR RRTRRAVTES
260 270 280 290 300
APNVEYHDVK GDMIQSVTTS FDDTSRLLTW TINLTPRQVK SNLGALVSIS
310 320 330 340 350
GNQETRTVTI NGKNAANGGV YNSGGAWNLY TGESVNNNVL RITTQVNDTG
360 370 380 390 400
GEVKLGLRLV TSDKKITKTN LPLEFSQVAA TTNGSWDKAG YNTTIVEKDT
410 420 430 440 450
ERPVVNVPSE ITVYRGESFE YFATVTDNSN AFDLAKTVVR WLYNNQPGRG
460 470 480 490 500
TEWLQYSVTQ VGNQLKVRIF GNVPIDTTIG DYTRYVVATD AAGNVNATQT
510 520 530 540 550
EMGNAAVDKT SVNGQFKLII RFRIKTPENT VFVNNPNQLT EVEKNLVREA
560 570 580 590 600
VKKSNPDLRA QDVLNSNYVT GITVSNNGTT TITYRDGRKD IIDGSKFIDT
610 620 630 640 650
RAGSISKSQS TSNSISVSLS KSESASASLV TSKLNSISSS ASVSASTSIS
660 670 680 690 700
TSGSVSASES ASTSSSVSAS ESASTSASVS ASESASTSAS VSASTSASTS
710 720 730 740 750
ASVSASTSAS TSASTSASKS ASTSASVSAS TSASTSASVS ASESASTSAS
760 770 780 790 800
VSASTSASTS ASVSASTSAS TSASVSASES ASTSASVSAS TSASTSASVS
810 820 830 840 850
ASESASTSAS VSASTSASTS ASVSASASAS TSASVSASTS ASTSASVSAS
860 870 880 890 900
ASASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES
910 920 930 940 950
ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS
960 970 980 990 1000
TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS VSASTSASTS
1010 1020 1030 1040 1050
ASVSASTSAS TSASVSASTS ASTSASVSAS ESASTSASVS ASESASTSAS
1060 1070 1080 1090 1100
VSASTSASTS ASVSASESAS TSASVSASES ASTSASESAS ESASTSASVS
1110 1120 1130 1140 1150
ASESASTSAS VSASESSSTS ASVSASESSS TSASVSASES ASTSASVSAS
1160 1170 1180 1190 1200
ESASTSASES ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
1210 1220 1230 1240 1250
VSTSASVSAS ESASTSASVS ASESASTSAS ESASESASTS ASVSASESAS
1260 1270 1280 1290 1300
TSASVSASES ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS
1310 1320 1330 1340 1350
ASVSASESAS TSASVSASES VSTSASVSAS ESASTSASVS ASESASTSAS
1360 1370 1380 1390 1400
ESASESASTS ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS
1410 1420 1430 1440 1450
ASESASTSAS VSASESASTS ASVSASESAS TSASVSASTS ASTSASVSAS
1460 1470 1480 1490 1500
ESASTSTSVS TSTSASTSAS VSASESASTS ASVSASESAS TSASVSASTS
1510 1520 1530 1540 1550
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS
1560 1570 1580 1590 1600
TSASVSASTS ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS
1610 1620 1630 1640 1650
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
1660 1670 1680 1690 1700
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS
1710 1720 1730 1740 1750
ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS
1760 1770 1780 1790 1800
ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
1810 1820 1830 1840 1850
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS
1860 1870 1880 1890 1900
TSASVSASES ASTSASVSAS TSTSTSASVS ASESASTSAS VSASESASTS
1910 1920 1930 1940 1950
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
1960 1970 1980 1990 2000
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS
2010 2020 2030 2040 2050
ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS
2060 2070 2080 2090 2100
ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASKS
2110 2120 2130 2140 2150
ASTSESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESVSTSASVS
2160 2170 2180 2190 2200
ASDSASISAS VLASESASTS ASVSASESAS TSASVSASES ASTSASVSAS
2210 2220 2230 2240 2250
ESASTSSSVS ASESASTSAS VSASESASTS ASVSASTSAS TSASVSASES
2260 2270 2280 2290 2300
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS
2310 2320 2330 2340 2350
TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS
2360 2370 2380 2390 2400
ASVSSSESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
2410 2420 2430 2440 2450
VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS
2460 2470 2480 2490 2500
ASESASTSAS VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS
2510 2520 2530 2540 2550
ESASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES
2560 2570 2580 2590 2600
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS
2610 2620 2630 2640 2650
TSASVSASMS ASTSASVSVS ESTSTSASVS ANESASTSAS VSASESASTS
2660 2670 2680 2690 2700
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
2710 2720 2730 2740 2750
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS
2760 2770 2780 2790 2800
ASTSASTSAS VSANESASTS ASVSASESAS TSASVSASES ASTSASVSAS
2810 2820 2830 2840 2850
ESASTSASVS ASESASTSAS VSASTSASTS ASVSANESAS TSASVSASES
2860 2870 2880 2890 2900
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASTSAS
2910 2920 2930 2940 2950
TSASVSASES ASTSASASAS ESASTSASVS ASESASTSAS VSASESASTS
2960 2970 2980 2990 3000
ASVSASESAS TNASVSVSES MSVSESLSLS ISTSVLHSQL NDIYESELYS
3010 3020 3030 3040 3050
LSLSESLSAS QSLSQSLSES QSSSASQSMH DRISKGQLPR TGESENKASI
3060 3070
LALGLGALGL AFKKRKKNES ED
Length:3,072
Mass (Da):285,769
Last modified:December 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i0B148372697CF7F2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY028381 Genomic DNA Translation: AAL13053.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY028381 Genomic DNA Translation: AAL13053.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QC5X-ray1.40X245-604[»]
3QC6X-ray1.90X245-604[»]
5IUCX-ray1.25A/B399-521[»]
6EF7X-ray1.03A399-521[»]
6EF9X-ray1.30A398-521[»]
6EFAX-ray1.60A399-601[»]
SMRiQ939N5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

IntActiQ939N5, 2 interactors

Protein family/group databases

UniLectiniQ939N5

Family and domain databases

InterProiView protein in InterPro
IPR044024, aRib
IPR019948, Gram-positive_anchor
IPR022263, KxYKxGKxW
IPR019931, LPXTG_anchor
IPR026465, Ser_adhes_glycop
PfamiView protein in Pfam
PF18938, aRib, 1 hit
PF00746, Gram_pos_anchor, 1 hit
TIGRFAMsiTIGR03715, KxYKxGKxW, 1 hit
TIGR04224, ser_adhes_Nterm, 1 hit
PROSITEiView protein in PROSITE
PS50847, GRAM_POS_ANCHORING, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGSPB_STRGN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q939N5
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: December 1, 2001
Last modified: June 2, 2021
This is version 73 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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