ID A0A3G6J8V3_9CORY Unreviewed; 902 AA.
AC A0A3G6J8V3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:AZA12444.1};
GN ORFNames=CCHOA_00045 {ECO:0000313|EMBL:AZA12444.1};
OS Corynebacterium choanae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1862358 {ECO:0000313|EMBL:AZA12444.1, ECO:0000313|Proteomes:UP000269019};
RN [1] {ECO:0000313|EMBL:AZA12444.1, ECO:0000313|Proteomes:UP000269019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=200CH {ECO:0000313|EMBL:AZA12444.1,
RC ECO:0000313|Proteomes:UP000269019};
RA Kleinhagauer T., Glaeser S.P., Spergser J., Ruckert C., Kaempfer P.,
RA Busse H.-J.;
RL Submitted (NOV-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; CP033896; AZA12444.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G6J8V3; -.
DR KEGG; ccho:CCHOA_00045; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000269019; 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:UP000269019};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 18..475
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 820..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 454..488
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 536..542
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 129
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 902 AA; 99600 MW; C985AF8A64BD7CC2 CRC64;
MSDDIHGGET LTDRIQPIDI AEEMQSSYID YAMSVIVGRA LPEVRDGLKP VHRRILYAMF
DSGYRPDRSY VKSSRPVADA MGKFHPHGDS AIYDTLVRLA QPWSMRYPLV DGQGNFGSPG
NDAAAAMRYT ECRLTPLAMQ MVRDIREDTV DFQPNYDGKN LEPVVLPARV PNLLMNGSGG
IAVGMATNIP PHNLRELGEA IFWLLENPDA EPKEALEACM ERVHGPDFPT AGLIVGDSGI
KDAYTTGRGS IRMRGVTAVE QEGSRQQIVI TELPYQVNPD NMISSIAEQI ESGKLTGISD
IQNESSDRIG MRIVIYLKRD AVPRVVLNNL YKHSQLQTSF GANMLSIVDG VPRTLRLDQM
LRNYVKHQIE VIVRRTRYRL QEAEKEAHIL RGLVKALDML DEVIALIRRS STPNVARTGL
MELLDIDEIQ ADAILAMQLR RLAAMERQKI IDRLAEIEAV IADLNDILAR EERQREIVRD
ELKEIVDKYG DDRRTEIIAA TGDVTEEDLI ARENVVVTIT STGYAKRTKV DAYRSQKRGG
KGVRGAELKQ DDVVRHFFVC STHDWILFFT NYGRVYRLKA YELPEASRTA RGQHVANLLS
FQPGETIAQV IQIQSYDDAD YLVLATAQGK VKKSKLTDYD SSRSGGLIAI NLAEDDRLIG
AALASADDDL LLVSDQGQAI RFTASDEALR PMGRATAGVR GMRFRGDDQM LAMCVVREGG
SLLVATSGGY GKRTKLEEYP TKNRGGLGVV TFKYTPKRGK LIGALTVDDD DQIFAITSAG
GVIRTEVGQI RPSSRQTMGV RLVNLEKGVE LLAIDRNVEE EGEETAEAVA HGEQPGRQRG
AEQTVDDAVE TITPATATEK TDASGVPIDD SGQTPEVLES TEHGTSLLDE DGNLADTDDE
QE
//
