ID A0A3L7ATJ4_9MICO Unreviewed; 855 AA.
AC A0A3L7ATJ4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:RLP83454.1};
GN ORFNames=D9V34_05410 {ECO:0000313|EMBL:RLP83454.1};
OS Mycetocola lacteus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Mycetocola.
OX NCBI_TaxID=76637 {ECO:0000313|EMBL:RLP83454.1, ECO:0000313|Proteomes:UP000269438};
RN [1] {ECO:0000313|EMBL:RLP83454.1, ECO:0000313|Proteomes:UP000269438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 11654 {ECO:0000313|EMBL:RLP83454.1,
RC ECO:0000313|Proteomes:UP000269438};
RA Li J.;
RL Submitted (OCT-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLP83454.1}.
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DR EMBL; RCUY01000004; RLP83454.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L7ATJ4; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000269438; Unassembled WGS sequence.
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:UP000269438};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 25..482
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 831..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..474
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 544..550
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 136
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 855 AA; 94282 MW; E82DB14FE80F538F CRC64;
MSDETNSEEN AEQIDHGVHG KIDQVDLRLE MQRSYLDYAM SVIVGRALPE VRDGLKPVHR
RVIYAMYDGG YRPEKAFSKC ARVVGDVMGQ FHPHGDSAIY DALVRLVQPW SLRYPLALGQ
GNFGSPGNDG AAAPRYTETK MAPLAMEMVR DIDEDTVDFQ DNYDGRTQEP AVLPARFPNL
LVNGSVGIAV GMATNIPPHN LREVAAGALW HLANPEAPRE EVLEALMERI KGPDFPTGAQ
ILGVNGIKDA YRTGRGSITM RAVVNVEEIQ GRTCLVVTEL PYQVNPDNLA IRIADLVKDG
KLAGIADIRD ETSGRTGQRL VIVLKRDAVA KVVLNNLYKH TQLQENFGAN MLAIVDGVPR
TLSLDGFITA WTAHQVDVIV RRTQFRLRKA EADAHIQRGY LAALDALDEV IALIRRSPDV
DKARTGLMEL LKVDQLQADA ILAMQLRRLA ALERQKIIDR AAELEREIAE YKAILDSPVR
QREIVSEELT EIVDRYGDDR RTEIMYGFDG DMNIEDLIPE EEMVLTVTRG GYIKRTRSDN
YRSQHRGGKG VKGAQLRADD VVEHFFVTTT HHWLLFFTNT GRVYRAKAYE VIEAGRDAKG
QHVANLLALQ PGEEIAQILD IRDYAAAEFL VLATRGGLVK KTSLSEYDTN RTGGIIAINL
REGDELVSAM LVEQDSDLML VSRQGMSIRF TADNEALRPM GRSTSGVTGM KFRGDDNLLS
ASVLPPAGEE GFVFVVTEGG FAKRTDVEQY RVQGRGGLGI KVAKLSEDRG ELAGALVVGD
EDEVLVVLAS GKVVRSAVAE VPAKGRDTMG VVFARFADND RIIALARNSD RNLDGQNGED
ETDAPTVTES SEKEE
//
