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Entry version 121 (07 Apr 2021)
Sequence version 1 (01 Jan 1990)
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Protein

Sporulation sigma-E factor-processing peptidase

Gene

spoIIGA

Organism
Bacillus subtilis (strain 168)
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

Probable aspartic protease that is responsible for the proteolytic cleavage of the RNA polymerase sigma E factor (SigE/spoIIGB) to yield the active peptide in the mother cell during sporulation. Responds to a signal from the forespore that is triggered by the extracellular signal protein SpoIIR.

6 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1831 Publication1

<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

  • aspartic-type endopeptidase activity Source: UniProtKB
  • peptidase activity Source: UniProtKB
  • protein self-association Source: UniProtKB

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

Molecular functionAspartyl protease, Hydrolase, Protease
Biological processSporulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
BSUB:BSU15310-MONOMER

Protein family/group databases

MEROPS protease database

More...
MEROPSi
A36.001

<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:
Sporulation sigma-E factor-processing peptidase (EC:3.4.23.-)
Alternative name(s):
Membrane-associated aspartic protease
Stage II sporulation protein GA
<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:spoIIGA
Ordered Locus Names:BSU15310
<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>OrganismiBacillus subtilis (strain 168)
<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 identifieri224308 [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 lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000001570 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei7 – 27HelicalSequence analysisAdd BLAST21
Transmembranei36 – 55HelicalSequence analysisAdd BLAST20
Transmembranei61 – 78HelicalSequence analysisAdd BLAST18
Transmembranei88 – 105HelicalSequence analysisAdd BLAST18
Transmembranei130 – 147HelicalSequence analysisAdd BLAST18

Keywords - Cellular componenti

Cell membrane, Membrane

<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

Does not affect the localization of SigE.1 Publication

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>Mutagenesisi164R → A: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi164R → I: Unaffected cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi164R → K: 75% reduced cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi165V → A or P: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi177H → A: Unaffected cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi180G → A: 70% reduced cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi180G → D: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi181L → A: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi182I → A or D: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi183D → A: Abolishes cleavage of wild-type SigE. Abolishes cleavage of SigE I-17 mutant. 2 Publications1
Mutagenesisi183D → E or N: Abolishes cleavage of SigE I-17 mutant. 2 Publications1
Mutagenesisi184S → A: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi184S → C: 2-fold reduced cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi184S → T: Unaffected cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi185G → A: 60% reduced cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi185G → V: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi190D → E: 2-fold reduced cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi230D → E: 2-fold reduced cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi245R → D: Abolishes cleavage of SigE. 1 Publication1
Mutagenesisi252Q → E: 60% reduced cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi259P → L: Unaffected cleavage of wild-type and K-25 mutant SigE in sporulating B.subtilis cells (PubMed:8002606). Abolishes cleavage of wild-type and K-25 mutant SigE when proteins are coexpressed in E.coli cells (PubMed:21362630). 2 Publications1
Mutagenesisi260D → A: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi260D → E: 2-fold reduced cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi261H → A or S: Unaffected cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi282T → E: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi283T → A: Nearly unaffected cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi284K → D: Reduced cleavage of SigE. 1 Publication1
Mutagenesisi286S → A: 80% reduced cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi294I → A: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi295I → A: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi296H → A, E, F, G, I, Q or S: Abolishes cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi296H → G: Abolishes cleavage of SigE I-17 mutant; when associated with N-298. 1 Publication1
Mutagenesisi298K → A: Unaffected cleavage of SigE I-17 mutant. 1 Publication1
Mutagenesisi298K → N: 80% reduced cleavage of SigE I-17 mutant. Abolishes cleavage of SigE I-17 mutant; when associated with G-296. 1 Publication1
Mutagenesisi302 – 309Missing : Abolishes cleavage of SigE I-17 mutant. 1 Publication8
Mutagenesisi307H → A: Unaffected cleavage of SigE I-17 mutant. 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 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_00000791791 – 309Sporulation sigma-E factor-processing peptidaseAdd BLAST309

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P13801

PRoteomics IDEntifications database

More...
PRIDEi
P13801

<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

Self-associates.

Interacts with SigE (Probable).

Interacts with SpoIIR.

Curated2 Publications

GO - Molecular functioni

  • protein self-association Source: UniProtKB

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
224308.BSU15310

<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

<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

Belongs to the peptidase U4 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG50301AF, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
IYLDVIW

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005081, SpoIIGA

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03419, Peptidase_U4, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF018571, SpoIIGA, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02854, spore_II_GA, 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.

P13801-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKIYLDVIWL LNFCFDALLL LLTAFILKRH VKKRRLVGGA FIGSSIVLLM
60 70 80 90 100
FTPFSPIVEH PAGKLAFSVV IVVVTFGFKR FRFFFQNLFS FYFATFLMGG
110 120 130 140 150
GIIGAHSLLQ SNSIVQNGVM ITNQTGFGDP ISWLFIVGGF PALWFFSKRR
160 170 180 190 200
IEDIETKNIQ YEERVSVQAD LGSQTLHVRG LIDSGNQLYD PLTKTPVMII
210 220 230 240 250
YIDKLEPIFG TAETMIIRNT DPLEAIEQLD DSFRFLDKMR LIPYRGVGQQ
260 270 280 290 300
NQFLLCVKPD HVTIMTKEEM ISADKCLIGI STTKLSADGE FDAIIHPKML

SGKAVKHVS
Length:309
Mass (Da):34,857
Last modified:January 1, 1990 - 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:i7B3453BA582C04EB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X17344 Genomic DNA Translation: CAA35225.1
AL009126 Genomic DNA Translation: CAB13405.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S08224, A29812

NCBI Reference Sequences

More...
RefSeqi
NP_389414.1, NC_000964.3
WP_003232163.1, NZ_JNCM01000035.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
CAB13405; CAB13405; BSU_15310

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
939984

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bsu:BSU15310

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|224308.179.peg.1669

<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
X17344 Genomic DNA Translation: CAA35225.1
AL009126 Genomic DNA Translation: CAB13405.1
PIRiS08224, A29812
RefSeqiNP_389414.1, NC_000964.3
WP_003232163.1, NZ_JNCM01000035.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

STRINGi224308.BSU15310

Protein family/group databases

MEROPSiA36.001

Proteomic databases

PaxDbiP13801
PRIDEiP13801

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
939984

Genome annotation databases

EnsemblBacteriaiCAB13405; CAB13405; BSU_15310
GeneIDi939984
KEGGibsu:BSU15310
PATRICifig|224308.179.peg.1669

Phylogenomic databases

eggNOGiENOG50301AF, Bacteria
OMAiIYLDVIW

Enzyme and pathway databases

BioCyciBSUB:BSU15310-MONOMER

Family and domain databases

InterProiView protein in InterPro
IPR005081, SpoIIGA
PfamiView protein in Pfam
PF03419, Peptidase_U4, 1 hit
PIRSFiPIRSF018571, SpoIIGA, 1 hit
TIGRFAMsiTIGR02854, spore_II_GA, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 nameiSP2G_BACSU
<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: P13801
<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: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 7, 2021
This is version 121 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

Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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