GYRA_MYCGO
ID GYRA_MYCGO Reviewed; 550 AA.
AC Q49467;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DNA gyrase subunit A;
DE EC=5.6.2.2 {ECO:0000250|UniProtKB:P0AES4};
DE Contains:
DE RecName: Full=Mgo GyrA intein;
DE Flags: Fragment;
GN Name=gyrA;
OS Mycobacterium gordonae.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1778;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GOR0 / 930835;
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.
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DR EMBL; Z68208; CAA92432.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49467; -.
DR SMR; Q49467; -.
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:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
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; Isomerase;
KW Nucleotide-binding; Protein splicing; Topoisomerase.
FT CHAIN <1..66
FT /note="DNA gyrase subunit A, 1st part"
FT /evidence="ECO:0000250|UniProtKB:P0AES4"
FT /id="PRO_0000034801"
FT CHAIN 67..486
FT /note="Mgo GyrA intein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034802"
FT CHAIN 487..>550
FT /note="DNA gyrase subunit A, 2nd part"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034803"
FT DOMAIN 192..332
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT ACT_SITE 66
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 550
SQ SEQUENCE 550 AA; 60537 MW; B71730590609E09C CRC64;
FRPDRSHAKS ARSVAETMGN YHPHGDASIY DTLVRMAQPW SLRYPLVDGQ GNFGSPGNDP
PAAMRYCLTG DALVRLPFGQ SMRIGDVAPG ARTNSDNAGE LKVLDRHGDP VFADRLFHSG
DHQTFRVQTA EGYEVTGTSN HPVLCLVNLA GVPTLLWMLI EEIRPDDYVV LQRAPPVESG
PANWRDAMEA LLLGAFISEG FMSESRAGFN NVDRDYFNAV VAAYDAVVGG KRYVAQRTIA
SGSVLNELDI HDVSALKGTR LGVLCGQRSA DKSVPEWLWQ SPAAVKRVFL QALFEGDGSC
SALPRNTIQV SYSTRSRQLA IDVQQMLLEF GVISRRYRHA VGEYKVVITN RAQAELFATQ
IGFGGAKQSK LTRILGSLPP CAGMDTNHVP GLAAFIRSHC DSEWVDKEWL RKHNIDRLSR
WRRDGAEILS RIANPDVRAI ATDLTDGRFY YAQVTSVTEA GVQPVYSLRV DSEDHAFLTN
GFVSHNTEAR LTPLAMEMLR EIDEETVDFI PNYDGRVQEP TVLPSRFPNL LANGSGGIAV
GMATNIPPHN
