GYRA_MYCMA
ID GYRA_MYCMA Reviewed; 473 AA.
AC O33149;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA gyrase subunit A;
DE EC=5.6.2.2 {ECO:0000250|UniProtKB:P0AES4};
DE Contains:
DE RecName: Full=Mma GyrA intein;
DE Flags: Fragment;
GN Name=gyrA;
OS Mycobacterium malmoense.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1780;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9493395; DOI=10.1099/00221287-144-2-589;
RA Sander P., Alcaide F., Richter I., Frischkorn K., Tortoli E., Springer B.,
RA Telenti A., Boettger E.C.;
RT "Inteins in mycobacterial GyrA are a taxonomic character.";
RL Microbiology 144:589-591(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: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; AJ002066; CAA05167.1; -; Genomic_DNA.
DR AlphaFoldDB; O33149; -.
DR SMR; O33149; -.
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; -; 1.
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; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
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..49
FT /note="DNA gyrase subunit A, 1st part"
FT /evidence="ECO:0000250|UniProtKB:P0AES4"
FT /id="PRO_0000034810"
FT CHAIN 50..469
FT /note="Mma GyrA intein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034811"
FT CHAIN 470..>473
FT /note="DNA gyrase subunit A, 2nd part"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034812"
FT DOMAIN 175..315
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT ACT_SITE 49
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT NON_TER 473
SQ SEQUENCE 473 AA; 52436 MW; 5DD88B4F50A2AEBC CRC64;
MGNYHPHGNA SIYNTLVRMA QPWSLRYPLV NGQGNFGSPG NNPPAAMRYC CTGDALVRLP
FGHSVRIGNF VPAACPNSDN AVNLKVLDRH GDPVVADQLF HSGEHQTYTV RTAEGYEVTG
TSNHPLLCLV DVGGVPTLLW KLIEEIRPDD HVVLQRTPPV EFGPADWHDV MEALLLGAFI
SEGFVSEVRA GFNNCDRDYF AMVVGAYDAV VGGRRYVSSR RIASGSTLHE LDIQNIKELK
EARLGDLCGQ RPADKSVPDW LWHSPAAVKR VFLQALFEGG GSCSALPRNM IQISYSTRSR
QLAVDVQQML LEFGIITRRY RHAVGEHKVL ITNRAQAELF ATRVGFGGAK QEKLTKILGS
MPPCAGMDSD HVPGLARFIR KHCGSRWVDK DWLNRHNVDR IQRWRTSGEK ILSHIADPDV
RAIATDLTDG RFYYAKVASV TEAGVQPVYS LRVDTDEHAF LTNGFVSHNT EAR
