GYRA_MYCXE
ID GYRA_MYCXE Reviewed; 327 AA.
AC P72065; P95323;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA gyrase subunit A;
DE EC=5.6.2.2 {ECO:0000250|UniProtKB:P0AES4};
DE Contains:
DE RecName: Full=Mxe GyrA intein;
DE Flags: Fragment;
GN Name=gyrA;
OS Mycobacterium xenopi.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1789;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IMM 5024;
RX PubMed=9335286; DOI=10.1128/jb.179.20.6378-6382.1997;
RA Telenti A., Southworth M., Alcaide F., Daugelat S., Jacobs W.R. Jr.,
RA Perler F.B.;
RT "The Mycobacterium xenopi GyrA protein splicing element: characterization
RT of a minimal intein.";
RL J. Bacteriol. 179:6378-6382(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF INTEIN.
RX PubMed=9437427; DOI=10.1038/nsb0198-31;
RA Klabunde T., Sharma S., Telenti A., Jacobs W.R. Jr., Sacchettini J.C.;
RT "Crystal structure of GyrA intein from Mycobacterium xenopi reveals
RT structural basis of protein splicing.";
RL Nat. Struct. Biol. 5:31-36(1998).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils closed
CC circular double-stranded (ds) DNA in an ATP-dependent manner to
CC modulate DNA topology and maintain chromosomes in an underwound state.
CC Negative supercoiling favors strand separation, and DNA replication,
CC transcription, recombination and repair, all of which involve strand
CC separation. Also able to catalyze the interconversion of other
CC topological isomers of dsDNA rings, including catenanes and knotted
CC rings. Type II topoisomerases break and join 2 DNA strands
CC simultaneously in an ATP-dependent manner.
CC {ECO:0000250|UniProtKB:P0AES4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000250|UniProtKB:P0AES4};
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains. In
CC the heterotetramer, GyrA contains the active site tyrosine that forms a
CC transient covalent intermediate with DNA, while GyrB binds cofactors
CC and catalyzes ATP hydrolysis. {ECO:0000250|UniProtKB:P0AES4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0AES4}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305|PubMed:9437427}.
CC -!- MISCELLANEOUS: Few gyrases are as efficient as E.coli at forming
CC negative supercoils. Not all organisms have 2 type II topoisomerases;
CC in organisms with a single type II topoisomerase this enzyme also has
CC to decatenate newly replicated chromosomes.
CC {ECO:0000250|UniProtKB:P0AES4}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family.
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DR EMBL; U67876; AAB81424.1; -; Genomic_DNA.
DR PDB; 1AM2; X-ray; 2.20 A; A=67-263.
DR PDB; 4OZ6; X-ray; 2.79 A; A=66-267, B=62-65.
DR PDBsum; 1AM2; -.
DR PDBsum; 4OZ6; -.
DR AlphaFoldDB; P72065; -.
DR SMR; P72065; -.
DR MEROPS; N10.008; -.
DR EvolutionaryTrace; P72065; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR Gene3D; 3.90.199.10; -; 2.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR Pfam; PF00521; DNA_topoisoIV; 2.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF56719; SSF56719; 2.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Autocatalytic cleavage; Cytoplasm; DNA-binding;
KW Isomerase; Nucleotide-binding; Protein splicing; Topoisomerase.
FT CHAIN <1..65
FT /note="DNA gyrase subunit A, 1st part"
FT /id="PRO_0000034813"
FT CHAIN 66..263
FT /note="Mxe GyrA intein"
FT /id="PRO_0000034814"
FT CHAIN 264..>327
FT /note="DNA gyrase subunit A, 2nd part"
FT /id="PRO_0000034815"
FT ACT_SITE 65
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AES4"
FT NON_TER 1
FT NON_TER 327
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1AM2"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 109..128
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:1AM2"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:1AM2"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:1AM2"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1AM2"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 226..251
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:1AM2"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:1AM2"
SQ SEQUENCE 327 AA; 35386 MW; EFAE9924D97068FB CRC64;
RPDRSHAKSA RSVAETMGNY HPHGDASIYD TLVRMAQPWS MRYPLVDGQG NFGSPGNDPP
AAMRYCITGD ALVALPEGES VRIADIVPGA RPNSDNAIDL KVLDRHGNPV LADRLFHSGE
HPVYTVRTVE GLRVTGTANH PLLCLVDVAG VPTLLWKLID EIKPGDYAVI QRSAFSVDCA
GFARGKPEFA PTTYTVGVPG LVRFLEAHHR DPDAQAIADE LTDGRFYYAK VASVTDAGVQ
PVYSLRVDTA DHAFITNGFV SHNTEAPLTP LAMEMLREID EETVDFIPNY DGRVQEPTVL
PSRFPNLLAN GSGGIAVGMA TNIPPHN
