ID A0A1G8EUZ8_9ACTN Unreviewed; 838 AA.
AC A0A1G8EUZ8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-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=SAMN05421505_12165 {ECO:0000313|EMBL:SDH73637.1};
OS Sinosporangium album.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Sinosporangium.
OX NCBI_TaxID=504805 {ECO:0000313|EMBL:SDH73637.1, ECO:0000313|Proteomes:UP000198923};
RN [1] {ECO:0000313|EMBL:SDH73637.1, ECO:0000313|Proteomes:UP000198923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 201354 {ECO:0000313|EMBL:SDH73637.1,
RC ECO:0000313|Proteomes:UP000198923};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 topoisomerase GyrA/ParC subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
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DR EMBL; FNCN01000021; SDH73637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8EUZ8; -.
DR STRING; 504805.SAMN05421505_12165; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000198923; 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:UP000198923};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 18..476
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 537..543
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 838 AA; 92585 MW; 8387BF13A1B3A81E CRC64;
MTEVNTPPGP PTDRIEPRDI QSEMQRSYMD YAMSVIVSRA LPDVRDGLKP VHRRVLYAMY
DGGYRPDRGY FKCSRVVGDV MGSYHPHGDA PIYDSLVRLA QPWSLRYPLV DGQGNFGSPG
NDPPAAMRYT ESKLAVIAME MLRDIDKDTV DFQPNYDGRS QEPVVLPARF PNLLVNGSGG
IAVGMATNIP PHNLREVAEG VKWALENPEA SDEETLEAMI ARVKGPDFPT RALIVGRRGI
EDAYRTGRGS ITMRAVVEVE EDSKGRQCLV VTELPYQVNP DNLALKIAEL VKVGKVTGIA
DVRDESSSRA GQRLVIVLKR DAVAKVVLNN LYKHTQLQDT FGANMLALVD GVPRTLRLDQ
FVRHYVAHQI EVVVRRTRYL LRKAQERAHI LSGLLRALER LDDVIALIRA SESAAAAQQG
LMGLLEIDEV QAQAILDMQL RKLAALERQQ IQDEHDALMA QIADYQDILS SEPRQRQIVG
DELSEMVAKF GDDRRTEIIA YDGDMSIEDL IAEEEMVVTI TRGGYTKRTR TDLYRAQKRG
GKGVRGAQLR QDDIVDHFFV TTTHHWLLFF TNKGRVYRVK AYELPDSGRD ARGQHLANLL
AMQPDETVME VLDLRDYQVA PYLVLATRSG LVKKTALSEY DSPRSGGLIA INLREDDEVI
AARLVSEHDD LLLVSKGAQS IRFTASDEAL RPMGRATSGV IGMRFVEGDE LLAMNRMADG
DDVLVATEGG YAKRTPAEQY PVQGRGGKGV LTAKIVSARG KLVGAVMVRP EDEIFAITSA
GGVIRTSAGE IKQSGRQTMG VRLMNLAEGD SVVALARNAD SLETSEALEA EESGENRA
//