Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 122 (29 Sep 2021)
Sequence version 1 (20 Dec 2005)
Previous versions | rss
Add a publicationFeedback
Protein

Bifunctional glutathionylspermidine synthetase/amidase

Gene

gss

Organism
Escherichia coli (strain K12)
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

Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. In vitro, the amidase active site also catalyzes hydrolysis of amide and ester derivatives of glutathione (e.g. glutathione ethyl ester and glutathione amide) but lacks activity toward acetylspermidine (N1 and N8) and acetylspermine (N1).

4 Publications

Miscellaneous

Gsp forms mixed disulfides with the thiols of a variety of E.coli proteins. These mixed disulfides represent a previously uncharacterized type of post-translational modification. The level of these proteins is increased by oxidative stress, which implies that Gsp might protect protein thiols against irreversible oxidation (PubMed:20530482).1 Publication
No metal ion is required for the amidase activity.1 Publication
Gsp hydrolysis to GSH and spermidine proceeds with formation of a glutathionyl acyl-enzyme intermediate, utilizing a cysteine residue as the catalytic nucleophile (PubMed:9398217). For Gsp synthesis, GSH is likely phosphorylated at one of two GSH-binding sites to form an acylphosphate intermediate that then translocates to the other site for subsequent nucleophilic addition of spermidine (PubMed:17124497).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

When exposed to oxidative stress, Gsp amidase activity is transiently inhibited in vivo by oxidation of the catalytic Cys-59 thiol to sulfenic acid; this modification does not affect Gsp synthetase activity. Gsp amidase activity is negatively autoregulated by the Gsp synthetase domain, and is activated by the Gsp synthetase substrates, GSH and ATP-Mg2+; the occupancy of the synthetase active site may initiate communication through the protein as manifest by the release of inhibition of the amidase activity. A tetrahedral phosphonate analog of glutathionylspermidine, designed as a mimic of the proposed tetrahedral intermediate for either reaction, inhibits the synthetase activity (Ki of 10 µM) but does not inhibit the amidase activity. Amidase activity is inhibited by iodoacetamide in vitro.3 Publications

<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>Kineticsi

kcat is 7 sec(-1) for Gsp synthetase activity at pH 6.8 and 2.1 sec(-1) for Gsp amidase activity at pH 7.5.1 Publication
  1. KM=100 µM for ATP (at pH 6.8)2 Publications
  2. KM=800 µM for glutathione (at pH 6.8)2 Publications
  3. KM=218 µM for glutathione2 Publications
  4. KM=60 µM for spermidine (at pH 6.8)2 Publications
  5. KM=20 µM for spermidine (at pH 7.5)2 Publications
  6. KM=76 µM for spermidine2 Publications
  7. KM=900 µM for glutathionylspermidine (at pH 7.5)2 Publications

pH dependencei

Optimum pH is around 6.8 for Gsp synthetase activity.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glutathione metabolism

This protein is involved in the pathway glutathione metabolism, which is part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the pathway glutathione metabolism and in Sulfur metabolism.

Pathwayi: spermidine metabolism

This protein is involved in the pathway spermidine metabolism, which is part of Amine and polyamine metabolism.
View all proteins of this organism that are known to be involved in the pathway spermidine metabolism and in Amine and polyamine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei58Glutathionylspermidine1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei59S-(gamma-glutamyl-cysteinyl-glycyl)-cysteine intermediate1 Publication1
Binding sitei64Glutathionylspermidine1
<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>Sitei131Increases nucleophilicity of active site Cys; for amidase activity1
Binding sitei149Glutathionylspermidine1
Binding sitei316Glutathione1
Sitei316Transition state stabilizer; for synthetase activity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi318Magnesium 11
Metal bindingi330Magnesium 11
Metal bindingi330Magnesium 21
Metal bindingi332Magnesium 21
Binding sitei335Glutathione1
Binding sitei391Spermidine1
Binding sitei392Glutathione1
Binding sitei446Glutathione1
Binding sitei498ATP1
Binding sitei533ATP1
Binding sitei582ATP1
Binding sitei610Spermidine1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi316 – 318ATP3
Nucleotide bindingi539 – 540ATP2
Nucleotide bindingi568 – 571ATP4
Nucleotide bindingi603 – 605ATP3

<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>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 functionHydrolase, Ligase, Multifunctional enzyme
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:GSP-MONOMER
MetaCyc:GSP-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.1.78, 2026
6.3.1.8, 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00204
UPA00819

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C51.A01

<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_and_taxonomy_section">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:
Bifunctional glutathionylspermidine synthetase/amidase
Short name:
GspSA
Including the following 2 domains:
Glutathionylspermidine amidase (EC:3.5.1.784 Publications)
Short name:
Gsp amidase
Alternative name(s):
Glutathionylspermidine amidohydrolase [spermidine-forming]
Glutathionylspermidine synthetase (EC:6.3.1.84 Publications)
Short name:
Gsp synthetase
Alternative name(s):
Glutathione:spermidine ligase [ADP-forming]
Gsp synthase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:gss
Synonyms:gsp
Ordered Locus Names:b2988, JW2956
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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
  • UP000000625 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

<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

Cells lacking this gene do not produce Gsp under anaerobic conditions. Cells lacking both this gene and glutaredoxin (grxA or grxB) become hypersensitive to H2O2; they are even more susceptible to oxidative damage than the single mutant lacking glutaredoxin only.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi59C → A: Loss of amidase activity. 1 Publication1
Mutagenesisi173C → A: No effect on amidase activity. 1 Publication1
Mutagenesisi316R → E: Loss of synthetase activity. 1
Mutagenesisi335S → A: 3.6-fold decrease in GSH affinity, 1.6-fold decrease in spermidine activity, and 1.3-fold decrease in synthetase activity. 1 Publication1
Mutagenesisi337S → A: No effect on GSH and spermidine affinity, but 2-fold decrease in synthetase activity. 1 Publication1
Mutagenesisi338C → A: 10-fold decrease in GSH affinity, 5-fold decrease in spermidine activity, but no effect on synthetase activity. 1 Publication1
Mutagenesisi391E → A: 2-fold decrease in GSH affinity, 60-fold decrease in spermidine activity, and 10-fold decrease in synthetase activity. 1 Publication1
Mutagenesisi392E → A: 33-fold decrease in GSH affinity, 13-fold decrease in spermidine activity, and 6-fold decrease in synthetase activity. 1 Publication1
Mutagenesisi441T → A: 3-fold decrease in GSH affinity, 21-fold decrease in spermidine activity, and 17-fold decrease in synthetase activity. 1 Publication1
Mutagenesisi538R → A: 6-fold decrease in GSH affinity, 2.4-fold decrease in spermidine activity, and 4-fold decrease in synthetase activity. 1 Publication1
Mutagenesisi598R → A: 10-fold increase in GSH affinity, 9-fold decrease in spermidine activity, and 15-fold decrease in synthetase activity. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00000704432 – 619Bifunctional glutathionylspermidine synthetase/amidaseAdd BLAST618

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 residuei59Cysteine sulfenic acid (-SOH); transient1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Oxidation of Cys-59 to sulfenic acid during oxidative stress selectively inhibits the amidase activity which leads to a rapid increase in the amounts of intracellular Gsp and Gsp S-thiolated proteins (GspSSPs).1 Publication

Keywords - PTMi

Oxidation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AES0

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

More...
PaxDbi
P0AES0

PRoteomics IDEntifications database

More...
PRIDEi
P0AES0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression level is unaffected by H2O2; however Gsp rapidly accumulates in E.coli in the presence of H2O2.

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261180, 18 interactors
851792, 4 interactors

Database of interacting proteins

More...
DIPi
DIP-36018N

Protein interaction database and analysis system

More...
IntActi
P0AES0, 14 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2988

<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

1619
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
P0AES0

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0AES0

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini34 – 176Peptidase C51PROSITE-ProRule annotationAdd BLAST143

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>Regioni2 – 195Gsp amidaseAdd BLAST194
Regioni78 – 81Glutathionylspermidine binding4
Regioni196 – 205Linker10
Regioni206 – 619Gsp synthetaseAdd BLAST414

<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

The two activities reside in distinct domains (N-terminal amidase and C-terminal synthetase). The two domains expressed independently are folded and functional; liberation of the amidase domain from the synthetase domain highly activates the amidase activity.2 Publications

<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

In the C-terminal section; belongs to the glutathionylspermidine synthase preATP-grasp family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0754, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_478805_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AES0

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AES0

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007921, CHAP_dom
IPR005494, GSPS_pre-ATP-grasp-like_dom
IPR038765, Papain-like_cys_pep_sf
IPR016185, PreATP-grasp_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05257, CHAP, 1 hit
PF03738, GSP_synth, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52440, SSF52440, 1 hit
SSF54001, SSF54001, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50911, CHAP, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P0AES0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKGTTSQDA PFGTLLGYAP GGVAIYSSDY SSLDPQEYED DAVFRSYIDD
60 70 80 90 100
EYMGHKWQCV EFARRFLFLN YGVVFTDVGM AWEIFSLRFL REVVNDNILP
110 120 130 140 150
LQAFPNGSPR APVAGALLIW DKGGEFKDTG HVAIITQLHG NKVRIAEQNV
160 170 180 190 200
IHSPLPQGQQ WTRELEMVVE NGCYTLKDTF DDTTILGWMI QTEDTEYSLP
210 220 230 240 250
QPEIAGELLK ISGARLENKG QFDGKWLDEK DPLQNAYVQA NGQVINQDPY
260 270 280 290 300
HYYTITESAE QELIKATNEL HLMYLHATDK VLKDDNLLAL FDIPKILWPR
310 320 330 340 350
LRLSWQRRRH HMITGRMDFC MDERGLKVYE YNADSASCHT EAGLILERWA
360 370 380 390 400
EQGYKGNGFN PAEGLINELA GAWKHSRARP FVHIMQDKDI EENYHAQFME
410 420 430 440 450
QALHQAGFET RILRGLDELG WDAAGQLIDG EGRLVNCVWK TWAWETAFDQ
460 470 480 490 500
IREVSDREFA AVPIRTGHPQ NEVRLIDVLL RPEVLVFEPL WTVIPGNKAI
510 520 530 540 550
LPILWSLFPH HRYLLDTDFT VNDELVKTGY AVKPIAGRCG SNIDLVSHHE
560 570 580 590 600
EVLDKTSGKF AEQKNIYQQL WCLPKVDGKY IQVCTFTVGG NYGGTCLRGD
610
ESLVIKKESD IEPLIVVKK
Length:619
Mass (Da):70,532
Last modified:December 20, 2005 - 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:i07FB43D8A0B2933C
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
U23148 Genomic DNA Translation: AAC43339.1
U28377 Genomic DNA Translation: AAA69155.1
U00096 Genomic DNA Translation: AAC76024.1
AP009048 Genomic DNA Translation: BAE77049.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A57538

NCBI Reference Sequences

More...
RefSeqi
NP_417462.1, NC_000913.3
WP_001297309.1, NZ_SSZK01000023.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC76024; AAC76024; b2988
BAE77049; BAE77049; BAE77049

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
61731136
947474

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2956
eco:b2988

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3741

<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
U23148 Genomic DNA Translation: AAC43339.1
U28377 Genomic DNA Translation: AAA69155.1
U00096 Genomic DNA Translation: AAC76024.1
AP009048 Genomic DNA Translation: BAE77049.1
PIRiA57538
RefSeqiNP_417462.1, NC_000913.3
WP_001297309.1, NZ_SSZK01000023.1

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 entryMethodResolution (Å)ChainPositionsPDBsum
2IO7X-ray2.70A/B1-619[»]
2IO8X-ray2.10A/B1-619[»]
2IO9X-ray2.20A/B1-619[»]
2IOAX-ray2.80A/B1-619[»]
2IOBX-ray2.20A/B1-619[»]
3A2YX-ray1.95A1-197[»]
3A2ZX-ray1.50A1-197[»]
3A30X-ray2.20A1-197[»]
3O98X-ray2.80A/B1-619[»]
SMRiP0AES0
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261180, 18 interactors
851792, 4 interactors
DIPiDIP-36018N
IntActiP0AES0, 14 interactors
STRINGi511145.b2988

Protein family/group databases

MEROPSiC51.A01

Proteomic databases

jPOSTiP0AES0
PaxDbiP0AES0
PRIDEiP0AES0

Genome annotation databases

EnsemblBacteriaiAAC76024; AAC76024; b2988
BAE77049; BAE77049; BAE77049
GeneIDi61731136
947474
KEGGiecj:JW2956
eco:b2988
PATRICifig|1411691.4.peg.3741

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB2720

Phylogenomic databases

eggNOGiCOG0754, Bacteria
HOGENOMiCLU_478805_0_0_6
InParanoidiP0AES0
PhylomeDBiP0AES0

Enzyme and pathway databases

UniPathwayiUPA00204
UPA00819
BioCyciEcoCyc:GSP-MONOMER
MetaCyc:GSP-MONOMER
BRENDAi3.5.1.78, 2026
6.3.1.8, 2026

Miscellaneous databases

EvolutionaryTraceiP0AES0

Protein Ontology

More...
PROi
PR:P0AES0

Family and domain databases

InterProiView protein in InterPro
IPR007921, CHAP_dom
IPR005494, GSPS_pre-ATP-grasp-like_dom
IPR038765, Papain-like_cys_pep_sf
IPR016185, PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF05257, CHAP, 1 hit
PF03738, GSP_synth, 1 hit
SUPFAMiSSF52440, SSF52440, 1 hit
SSF54001, SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS50911, CHAP, 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 nameiGSP_ECOLI
<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: P0AES0
Secondary accession number(s): P43675, Q2M9K7
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 29, 2021
This is version 122 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again