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

<p>Describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the ‘Names and taxonomy’ section.</p><p><a href='../manual/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

<p>Provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.</p><p><a href='../manual/cofactor' target='_top'>More...</a></p>Cofactorⁱ

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	11 – 11	1	ATPUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	51 – 51	1	ATPUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	78 – 78	1	ATPUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	344 – 344	1	ATPUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	433 – 433	1	Magnesium 1; catalyticUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>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><p><a href='../manual/site' target='_top'>More...</a></p>Sitei	458 – 458	1	Interaction with DNAUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>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><p><a href='../manual/site' target='_top'>More...</a></p>Sitei	461 – 461	1	Interaction with DNAUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	506 – 506	1	Magnesium 1; catalyticUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	506 – 506	1	Magnesium 2UniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	508 – 508	1	Magnesium 2UniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>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><p><a href='../manual/site' target='_top'>More...</a></p>Sitei	513 – 513	1	Interaction with DNAUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939
<p>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><p><a href='../manual/site' target='_top'>More...</a></p>Sitei	629 – 629	1	Interaction with DNAUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>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><p><a href='../manual/np_bind' target='_top'>More...</a></p>Nucleotide bindingi	118 – 124	7	ATPUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. ATP binding Source: UniProtKB-HAMAP
2. DNA binding Source: UniProtKB-HAMAP
3. DNA topoisomerase type II (ATP-hydrolyzing) activity Source: UniProtKB-HAMAP
4. magnesium ion binding Source: UniProtKB-HAMAP

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. chromosome segregation Source: UniProtKB-HAMAP
2. DNA topological change Source: UniProtKB-HAMAP

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Ligandⁱ

Enzyme and pathway databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

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

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. chromosome Source: InterPro

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

<p>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 ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

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

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>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><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	427 – 541	115	ToprimUniRule annotation <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More…</a></p> Automatic assertion according to rulesi HAMAP-Rule:MF_00939			Add BLAST

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MSKKEININN YNDDAIQVLE GLDAVRKRPG MYIGSTDGAG LHHLVWEIVD 
        60         70         80         90        100
NAVDEALSGF GDRIDVTINK DGSLTVQDHG RGMPTGMHAM GIPTVEVIFT 
       110        120        130        140        150
ILHAGGKFGQ GGYKTSGGLH GVGSSVVNAL SSWLEVEITR DGAVYKQRFE 
       160        170        180        190        200
NGGKPVTTLK KIGTALKSKT GTKVTFMPDA TIFSTTDFKY NTISERLNES 
       210        220        230        240        250
AFLLKNVTLS LTDKRTDEAI EFHYENGVQD FVSYLNEDKE ILTPVLYFEG 
       260        270        280        290        300
EDNGFQVEVA LQYNDGFSDN ILSFVNNVRT KDGGTHETGL KSAITKVMND 
       310        320        330        340        350
YARKTGLLKE KDKNLEGSDY REGLAAVLSI LVPEEHLQFE GQTKDKLGSP 
       360        370        380        390        400
LARPVVDGIV ADKLTFFLME NGELASNLIR KAIKARDARE AARKARDESR 
       410        420        430        440        450
NGKKNKKDKG LLSGKLTPAQ SKNPAKNELY LVEGDSAGGS AKQGRDRKFQ 
       460        470        480        490        500
AILPLRGKVI NTAKAKMADI LKNEEINTMI YTIGAGVGAD FSIEDANYDK 
       510        520        530        540        550
IIIMTDADTD GAHIQTLLLT FFYRYMRPLV EAGHVYIALP PLYKMSKGKG 
       560        570        580        590        600
KKEEVAYAWT DGELEELRKQ FGKGATLQRY KGLGEMNADQ LWETTMNPET 
       610        620        630        640 
RTLIRVTIED LARAERRVNV LMGDKVEPRR KWIEDNVKFT LEEATVF 

Sequence databases

Genome annotation databases

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "Genome of the bacterium Streptococcus pneumoniae strain R6."
   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S., DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C., Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J., Lee L.N.

   , Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M., McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B., Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y., Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R., Rosteck P.R. Jr., Skatrud P.L., Glass J.I.
   J. Bacteriol. 183:5709-5717(2001) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
   Strain: ATCC BAA-255 / R6Imported

   <p>Information which has been imported from another database using automatic procedures.</p> <p><a href="/manual/evidences#ECO:0000313">More…</a></p> Automatic assertion inferred from database entriesⁱ

   • Proteomes:UP000000586
   .
   
2. "Fragment-to-hit-to-lead discovery of a novel pyridylurea scaffold of ATP competitive dual targeting type II topoisomerase inhibiting antibacterial agents."
   Basarab G.S., Manchester J.I., Bist S., Boriack-Sjodin P.A., Dangel B., Illingworth R., Sherer B.A., Sriram S., Uria-Nickelsen M., Eakin A.E.
   J. Med. Chem. 56:8712-8735(2013) [PubMed] [Europe PMC] [Abstract]
   Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-226.
3. "Thiazolopyridone ureas as DNA gyrase B inhibitors: optimization of antitubercular activity and efficacy."
   Kale R.R., Kale M.G., Waterson D., Raichurkar A., Hameed S.P., Manjunatha M.R., Kishore Reddy B.K., Malolanarasimhan K., Shinde V., Koushik K., Jena L.K., Menasinakai S., Humnabadkar V., Madhavapeddi P., Basavarajappa H., Sharma S., Nandishaiah R., Mahesh Kumar K.N.

   , Ganguly S., Ahuja V., Gaonkar S., Naveen Kumar C.N., Ogg D., Boriack-Sjodin P.A., Sambandamurthy V.K., de Sousa S.M., Ghorpade S.R.
   Bioorg. Med. Chem. Lett. 24:870-879(2014) [PubMed] [Europe PMC] [Abstract]
   Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-226.

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

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

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Technical termⁱ

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ