GYRA_MYCFV
ID GYRA_MYCFV Reviewed; 554 AA.
AC Q49166;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DNA gyrase subunit A;
DE EC=5.6.2.2 {ECO:0000250|UniProtKB:P0AES4};
DE Contains:
DE RecName: Full=Mfl GyrA intein;
DE Flags: Fragment;
GN Name=gyrA;
OS Mycolicibacterium flavescens (Mycobacterium flavescens).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1776;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FLA0 / 930991;
RX PubMed=8622949; DOI=10.1073/pnas.93.8.3410;
RA Fsihi H., Vincent V., Cole S.T.;
RT "Homing events in the gyrA gene of some mycobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3410-3415(1996).
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:0000250}.
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. {ECO:0000305}.
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DR EMBL; Z68209; CAA92433.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49166; -.
DR SMR; Q49166; -.
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:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.28.10; -; 1.
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; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
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 Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF55608; SSF55608; 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; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Autocatalytic cleavage; Cytoplasm; DNA-binding; Endonuclease;
KW Hydrolase; Intron homing; Isomerase; Nuclease; Nucleotide-binding;
KW Protein splicing; Topoisomerase.
FT CHAIN <1..69
FT /note="DNA gyrase subunit A, 1st part"
FT /evidence="ECO:0000250|UniProtKB:P0AES4"
FT /id="PRO_0000034798"
FT CHAIN 70..490
FT /note="Mfl GyrA intein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034799"
FT CHAIN 491..>554
FT /note="DNA gyrase subunit A, 2nd part"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034800"
FT DOMAIN 195..335
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT ACT_SITE 69
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 554
SQ SEQUENCE 554 AA; 60953 MW; EB8209BBCAAD7765 CRC64;
RGIFRPDRSH AKSARSVAET MGNYHPHGDA SIYDTLVRMA QPWSLRYPLV DGQGNFGSPG
NDPPAAMRYC VTGDALVRLP FGQSVRLRDV VAGARSSSDN AIDLKVLNRH GDPVVADKLF
HSGEHETYTV RTAEGYEVTG TANHPLLCLV DVGGVPTLLW KLTEEIRPGD HVVLQRTPPT
EFGPADWQDA FEALHLGAFI SEGFVSENRA GFNNLDREFF NAVLTAYDTI VGGPRYVSSR
TIASDSLLHE LDVHNLTALK KSRLGELVGQ RSADKAVPEW LWKAPAVVKR VFLQALFEGD
GSCSALPRNT IQVSYSTRSG RLAKDIQQML LEFGVISRRY VHATGEHKVV LTSRAQAELF
AAQIGFGGIK QAKLQGLLDA LPQAAAGRDG DYVPGLAQFV RKHSGSRWVD KDWLNRHNID
RLSRWQRDGA EILGRIADPD VRAIAQELTD GRFYYARVAS VTDSGVQPVY SLRVDTDDHS
FITNGFVSHN TEARLTPLAM EMLREIDEET VDFIPNYDGR VQEPTVLPSR FPNLLANGSG
GIAVGMATNI PPHN
