GYRA_MYCKA
ID GYRA_MYCKA Reviewed; 549 AA.
AC Q49608;
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=Mka GyrA intein;
DE Flags: Fragment;
GN Name=gyrA;
OS Mycobacterium kansasii.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1768;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KANS0 / 930908;
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; Z68207; CAA92431.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49608; -.
DR SMR; Q49608; -.
DR STRING; 1768.B1T50_14880; -.
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..65
FT /note="DNA gyrase subunit A, 1st part"
FT /evidence="ECO:0000250|UniProtKB:P0AES4"
FT /id="PRO_0000034804"
FT CHAIN 66..485
FT /note="Mka GyrA intein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034805"
FT CHAIN 486..>549
FT /note="DNA gyrase subunit A, 2nd part"
FT /evidence="ECO:0000250"
FT /id="PRO_0000034806"
FT DOMAIN 191..331
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00273"
FT ACT_SITE 65
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000250"
FT NON_TER 1
FT NON_TER 549
SQ SEQUENCE 549 AA; 61051 MW; 5560B6B771B8B43F CRC64;
RPARSHAKSA RSVAETMGNY HPHGDASIYD TLVRMAQPWS LRYPLVDGQG NFGSPGNVPP
AAMRYCVTGD ALVRLPFGQS MRIADVVPGA RPNSDNAVEL KVLDRHGNPV AADRLFHSGD
HQTYMVRTAE GYEVTGTANH PLLCLVDVGG VPTLLWKLIE EIHPDDYVAL QRTPPMELGP
ADWHDTMEAL LLGAFISEGC VSETRAGFAN LDRDYFTMVA RAYDAVVGDK RDVYQQTIAS
GSLQHTLYTQ NVTALKQSRL WQILGMRSAD TYVPEWMWHS PAAVKRVFLQ ALFEGDGSCS
RRPHNTIQIS YNTVSKQLAM DVQQMLLEFG VISRRYLHAA GEYKVVITDR AQAELFPKQI
GFGGAKQTEL SKILAAMPPC AGRDSDHVPG LARFIRRHCD SRWVDKEWLH KHNIDHLSRW
RRDGAEILSH IADPDVRTIA TDLTDGRFYY ARVASVTDTG VQPVYSLRVD TDDHAFLTNG
FVSHNTEARL TPLAMEMLRE IDEETVDFIP NYDGRVQEPT VLPSRFPNLL ANGSGGIAVG
MATNIPPHN
