GYRA_MYCSM
ID GYRA_MYCSM Reviewed; 854 AA.
AC Q59556;
DT 17-FEB-2016, 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 {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000312|EMBL:CAA58885.1};
OS Mycolicibacterium smegmatis (Mycobacterium smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1772;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND
RP SUBUNIT.
RC STRAIN=ATCC 27204 / DSM 43464 / SN2;
RX PubMed=8574396; DOI=10.1099/13500872-141-12-3029;
RA Madhusudan K., Nagaraja V.;
RT "Mycobacterium smegmatis DNA gyrase: cloning and overexpression in
RT Escherichia coli.";
RL Microbiology 141:3029-3037(1995).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR
RP LOCATION, AND DNA-BINDING.
RC STRAIN=ATCC 27204 / DSM 43464 / SN2;
RX PubMed=12000834; DOI=10.1093/nar/30.10.2144;
RA Manjunatha U.H., Dalal M., Chatterji M., Radha D.R., Visweswariah S.S.,
RA Nagaraja V.;
RT "Functional characterisation of mycobacterial DNA gyrase: an efficient
RT decatenase.";
RL Nucleic Acids Res. 30:2144-2153(2002).
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 also catalyzes the interconversion of other topological isomers of
CC double-stranded DNA rings, including catenanes (PubMed:8574396,
CC PubMed:12000834). At comparable concentrations has a stronger
CC decatenation activity than E.coli, which is inhibited by ciprofloxacin
CC and novobiocin (PubMed:12000834). Cleaves dsDNA at the sequence 5'-
CC AT/GGCC-3', leaving a 4 base overhang (PubMed:12000834). Relaxes
CC negatively supercoiled DNA in an ATP-independent manner
CC (PubMed:12000834). {ECO:0000269|PubMed:12000834,
CC ECO:0000269|PubMed:8574396}.
CC -!- FUNCTION: Negative supercoiling favors strand separation, and DNA
CC replication, transcription, recombination and repair, all of which
CC involve strand separation. Type II topoisomerases break and join 2 DNA
CC strands simultaneously in an ATP-dependent manner. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01897,
CC ECO:0000269|PubMed:12000834};
CC -!- ACTIVITY REGULATION: DNA supercoiling is inhibited by the coumarin
CC antibiotic novobiocin (PubMed:8574396). Also inhibited by the
CC fluoroquinolones ciprofloxacin and moxifloxacin (PubMed:12000834).
CC {ECO:0000269|PubMed:12000834, ECO:0000269|PubMed:8574396}.
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains
CC (PubMed:12000834, PubMed:8574396). In the heterotetramer, GyrA contains
CC the active site tyrosine that forms a transient covalent intermediate
CC with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis.
CC {ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:12000834,
CC ECO:0000305|PubMed:8574396}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897,
CC ECO:0000269|PubMed:12000834}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR EMBL; X84077; CAA58885.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59556; -.
DR SMR; Q59556; -.
DR BindingDB; Q59556; -.
DR ChEMBL; CHEMBL6061; -.
DR eggNOG; COG0188; Bacteria.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IDA:UniProtKB.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 1.
DR Gene3D; 3.90.199.10; -; 1.
DR HAMAP; MF_01897; GyrA; 1.
DR InterPro; IPR005743; GyrA.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Topoisomerase.
FT CHAIN 1..854
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000435479"
FT MOTIF 537..543
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 129
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 854 AA; 94925 MW; AEC088EDD51323A1 CRC64;
MTDTTLPPEG EAHDRIEPVD IQQEMQRSYI DYAMSVIVGR ALPEVRDGLK PVHRRVLYAM
YDSASSDRSH AKSARSVAET MGNYHPHGDA SIYDTLVRMA QPWSLRYPLV DGQGNFGSPG
NDPPAAMRYT EARLTPLAME MLREIDEETV DFIPNYDGRV QEPTVLPSRF PNLLANGSRG
IAVGMATNNP PHNLGELAEA VYWCLENYEA DEEATCEAVM ERVKGPDFPT SGLIVGTQGI
EDTYKTGRGS IKMRGVVEIE EDSRGRTSIV ITELPYQVNH DNFITSIAEQ VRDGKLAGIS
NIEDQSSDRV GLRIVVELKR DAVAKVVLNN LYKHTQLQTS FGANMLSIVD GVPRTLRLDQ
LIRLYVDHQL DVIVRRTRYR LRKANERAHI LRGLVKALDA LDEVIALIRA SQTVDIARAG
LIELLDIDDI QAQAILDMQL RRLAALERQK IVDDLAKIEA EIADLEDILA KPERQRGIVR
DELKEIVDKH GDARRTRIVP ADGQVSDEDL IAREDVVVTI TETGYAKRTK TDLYHSQKRG
GKGVQGAGLK QDDMVNHFFV CSTHDWILFF TTQGRVYRAK AYELPEASRT ARGQHVANLL
AFQPEERIAQ VIQIKSYEDA PYLVLATRNG LVKKSKLSDF DSNRSGGIVA INLREGDELV
GAVLCSAEDD LLLVSANRQS IRFSATDEAL RPMGRATSGV QGMRFNEDDR LLSLNVVRPD
TYLLVATSGG YAKRTSIDEY SVQGRGGKGI LTIQYDRKRG SLVGALIVDD DTELYAITST
GGVIRTAARQ VRKAGRQTKG VRLMNLAEGD TLIAIARNGR GRGGRVDQRI RRGHRRVTRG
VMETLRSRKV LGPS
