ID A0A3S9MZQ8_9FLAO Unreviewed; 839 AA.
AC A0A3S9MZQ8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897,
GN ECO:0000313|EMBL:AZQ44638.1};
GN ORFNames=EJ995_10455 {ECO:0000313|EMBL:AZQ44638.1};
OS Nonlabens ponticola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=2496866 {ECO:0000313|EMBL:AZQ44638.1, ECO:0000313|Proteomes:UP000279600};
RN [1] {ECO:0000313|EMBL:AZQ44638.1, ECO:0000313|Proteomes:UP000279600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ115 {ECO:0000313|EMBL:AZQ44638.1,
RC ECO:0000313|Proteomes:UP000279600};
RA Choi H.S., Jung J.;
RT "Complete genome of Nonlabens sp. MJ115.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|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:0000256|ARBA:ARBA00000185,
CC ECO:0000256|HAMAP-Rule:MF_01897};
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:0000256|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897}.
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:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC Rule:MF_01897}.
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DR EMBL; CP034549; AZQ44638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9MZQ8; -.
DR KEGG; noj:EJ995_10455; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000279600; Chromosome.
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; IEA:UniProt.
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; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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 NCBIfam; TIGR01063; gyrA; 1.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01897};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Reference proteome {ECO:0000313|Proteomes:UP000279600};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 10..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 434..482
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 523..529
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 839 AA; 94106 MW; DC185A92AD97663D CRC64;
MADGEKLIPI NIEDEMKSAY IDYSMSVIVS RALPDVRDGL KPVHRRVLYG MYELGVLSNR
GYKKSARIVG EVLGKYHPHG DTSVYDTMVR MAQEWSLRYM LVDGQGNFGS VDGDPPAAMR
YTEARMRKIS EEMLADIDKE TVDTQLNFDD TLSEPTVLPT KIPNLLVNGA SGIAVGMATN
MPPHNLTEVV DGTIAYIDNN DIEIDELIQH IKAPDFPTGG IIYGYDGVKD AMHTGRGRVK
IRGRVRIEEV KGRECILVDE LPYQVNKADM IKKTADLIND KKLEGISSIR DESDRKGMRI
VYVLKRDAIP NIVINKLYKH TALQSSFSVN NIALVNGRPE MLNVKDMIHH FVEHRHEVVV
RRTTYELRKA EERAHILEGL IIASDNIDEV IKLIRASSNG EEAREKLIER FDLSEIQARA
IVEMRLRQLT GLEQDKLRSE YDELIKTIAD LKDILDKKER RMAIIKEELE EVREKYGDER
RSQIEYAGGD LSIEDMIPDE QVVITISHAG YIKRTSLTEY KTQNRGGVGQ KASTTRDEDF
LEDIFVGTNH QYMLFFTEKG KCFWMRVYEI PEGSRTSKGR AIQNLINIEP DDSVKAVICT
QDIKDEEYIN SHYVIMCTKK GTVKKTSLEQ YSRPRTNGIN AITIKDGDTL LEAKLTTGDS
QIMLGLRSGK AIRFDEKKTR SMGRNASGVR GIRLADDNDE VIGMVAVNDP ESNILVVSEK
GYGKRSSLED YRETNRGGKG VKTISVTEKT GGLVALKNVQ DGDGLMIINK SGVAIRIDVS
DMRVMGRATQ GVRLINLKGN DSIAAVAKVA NDDDDEAADI VTDELTDRGT DLAKDDSEE
//
