DNA gyrase subunit A - Mycobacterium xenopi

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P72065 (GYRA_MYCXE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA gyrase subunit A
EC=5.99.1.3

Cleaved into the following chain:

Mxe gyrA intein

Gene names

Name:

gyrA

Organism

Mycobacterium xenopi

Taxonomic identifier

1789 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	327 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings By similarity. HAMAP-Rule MF_01897
Catalytic activity	ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP-Rule MF_01897
Subunit structure	Heterotetramer, composed of two GyrA and two GyrB chains. Within the heterotetramer, GyrA contains the active site tyrosine that forms a covalent intermediate with the DNA, while GyrB contributes the cofactor binding sites and catalyzes ATP hydrolysis By similarity.
Subcellular location	Cytoplasm Potential HAMAP-Rule MF_01897.
Post-translational modification	This protein undergoes a protein self splicing that involves a post-translational excision of the intervening region (intein) followed by peptide ligation. HAMAP-Rule MF_01897
Sequence similarities	Belongs to the topoisomerase GyrA/ParC subunit family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
PTM	Autocatalytic cleavage Protein splicing
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	DNA topological change Inferred from electronic annotation. Source: InterPro intein-mediated protein splicing Inferred from electronic annotation. Source: InterPro
Cellular_component	chromosome Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase type II (ATP-hydrolyzing) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

‹1 – 65

›65

DNA gyrase subunit A, 1st part HAMAP-Rule MF_01897

PRO_0000034813

Chain

66 – 263

198

Mxe gyrA intein HAMAP-Rule MF_01897

PRO_0000034814

Chain

264 – ›327

›64

DNA gyrase subunit A, 2nd part HAMAP-Rule MF_01897

PRO_0000034815

Sites

Active site

O-(5'-phospho-DNA)-tyrosine intermediate By similarity

Experimental info

Non-terminal residue

327

Secondary structure

327

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P72065 [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: EFAE9924D97068FB
Show »

FASTA

327

35,386

        10         20         30         40         50         60 
RPDRSHAKSA RSVAETMGNY HPHGDASIYD TLVRMAQPWS MRYPLVDGQG NFGSPGNDPP 

        70         80         90        100        110        120 
AAMRYCITGD ALVALPEGES VRIADIVPGA RPNSDNAIDL KVLDRHGNPV LADRLFHSGE 

       130        140        150        160        170        180 
HPVYTVRTVE GLRVTGTANH PLLCLVDVAG VPTLLWKLID EIKPGDYAVI QRSAFSVDCA 

       190        200        210        220        230        240 
GFARGKPEFA PTTYTVGVPG LVRFLEAHHR DPDAQAIADE LTDGRFYYAK VASVTDAGVQ 

       250        260        270        280        290        300 
PVYSLRVDTA DHAFITNGFV SHNTEAPLTP LAMEMLREID EETVDFIPNY DGRVQEPTVL 

       310        320 
PSRFPNLLAN GSGGIAVGMA TNIPPHN

« Hide

References

[1]	"The Mycobacterium xenopi GyrA protein splicing element: characterization of a minimal intein." Telenti A., Southworth M., Alcaide F., Daugelat S., Jacobs W.R. Jr., Perler F.B. J. Bacteriol. 179:6378-6382(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IMM 5024.
[2]	"Crystal structure of GyrA intein from Mycobacterium xenopi reveals structural basis of protein splicing." Klabunde T., Sharma S., Telenti A., Jacobs W.R. Jr., Sacchettini J.C. Nat. Struct. Biol. 5:31-36(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF INTEIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U67876 Genomic DNA. Translation: AAB81424.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AM2	X-ray	2.20	A	67-263	[»]

ProteinModelPortal

P72065.

SMR

P72065. Positions 3-65, 67-327.

ModBase

Search...

Protein family/group databases

MEROPS

N10.008.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.90.199.10. 2 hits.

HAMAP

MF_01897. GyrA.

InterPro

IPR003586. Hint_dom_C.
IPR003587. Hint_dom_N.
IPR006141. Intein_splice_site.
IPR002205. Topo_IIA_A/C.
IPR013758. Topo_IIA_A/C_ab.
IPR013760. Topo_IIA_like_dom.
[Graphical view]

Pfam

PF00521. DNA_topoisoIV. 2 hits.
[Graphical view]

SMART

SM00305. HintC. 1 hit.
SM00306. HintN. 1 hit.
SM00434. TOP4c. 1 hit.
[Graphical view]

SUPFAM

SSF56719. Topo_IIA_cen. 2 hits.

TIGRFAMs

TIGR01443. intein_Cterm. 1 hit.
TIGR01445. intein_Nterm. 1 hit.

PROSITE

PS50818. INTEIN_C_TER. 1 hit.
PS50817. INTEIN_N_TER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P72065.

Entry information

Entry name

GYRA_MYCXE

Accession

Primary (citable) accession number: P72065
Secondary accession number(s): P95323

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Intein-containing proteins

List of intein-containing protein entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Family and domain databases

Other

Entry information

Relevant documents