ID A0A2N3YMD6_9MICO Unreviewed; 899 AA.
AC A0A2N3YMD6;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 ORFNames=ATL31_2819 {ECO:0000313|EMBL:PKW27968.1};
OS Phycicoccus duodecadis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Phycicoccus.
OX NCBI_TaxID=173053 {ECO:0000313|EMBL:PKW27968.1, ECO:0000313|Proteomes:UP000233781};
RN [1] {ECO:0000313|EMBL:PKW27968.1, ECO:0000313|Proteomes:UP000233781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12806 {ECO:0000313|EMBL:PKW27968.1,
RC ECO:0000313|Proteomes:UP000233781};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 Actinobacteria strains.";
RL Submitted (DEC-2017) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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:PKW27968.1}.
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DR EMBL; PJNE01000001; PKW27968.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N3YMD6; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000233781; 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}; 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:UP000233781};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 15..472
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 804..899
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..899
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 899 AA; 98187 MW; 486AAEDA37DB4683 CRC64;
MTEQPPIETD RTEPIDLNTE MQRSYIEYAM SVIVSRALPD VRDGLKPVHR RVLYAMYDGG
YRPDRGFNKC SRVVGDVMGQ YHPHGDSAIY DALVRLVQDW SLRYPLVQGQ GNFGSPGDDP
AAAPRYTECR MAPLSMEMVR DIDEETVDFR PNYDGKTLEP SVLPSRFPNL LVNGSSGIAV
GMATQIPPHN LREVAAAAEW VLAHPDATRD EMLEAVMREI KGPDFPTGAL IMGTKGLDDA
YRTGRGSVIM RAVVEVEEIQ GRQCLVVTEL PYQVNPDSLA QKIAEHVKDG RLSGIADIRD
ETSGRTGQRL VIVLKRDAVA KVVLNNLFKH TQLQTNFGAN MLALVDGVPR TLPIDAFIRH
WVDHQLDVIQ RRTAYRLRRA EERIHILRGL LKALDALDEV IALIRRSPDV EAARTGLIEL
LEIDEVQAQA ILDMQLRRLA ALERQKIIDD HDELQAMIED FTDILAKPGR QRDIVSEELA
EIVKKFGDDR RTKITHFDGD MSMEDLIPEE DVVVTITRGG YAKRTRVDAY RAQKPGGRGV
RGAQLRGEDM VEHFFATTSH HWLLFFTNLG RVYRAKAYEL PDAGRDSKGQ HVANLLAFQP
GEEIAQVLAI RSYEDAPYLV LATRGGLVKK TRLSEYDSPR TGGLIAVNLR DDDELVGVGL
VSPSDDLLLV SRKGMSVRFH ADDAQLRPMG RGTSGVTGMK FRGDDTLLAM AVIADGTEPD
VFVVFENGMA KRTSATEWNA KGRATLGVAV AKITDRNGDL AGALTTTGDD ELLIVFEKGN
IVRATTSGIA PKGRNTQGVI LVKPPKGDRV KAVARNPEKD EDDAVGEADE APVTGGDGAV
SGAEGAGAGD VAGDEALEAS GGAGEESVTT AESGAARVAD DGDDAVPSDD ETTDRGGRE
//
