ID A0A1Y0EBA9_9RHOB Unreviewed; 908 AA.
AC A0A1Y0EBA9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:ARU00788.1};
GN ORFNames=LOKVESSMR4R_01471 {ECO:0000313|EMBL:ARU00788.1};
OS Yoonia vestfoldensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=245188 {ECO:0000313|EMBL:ARU00788.1, ECO:0000313|Proteomes:UP000195273};
RN [1] {ECO:0000313|EMBL:ARU00788.1, ECO:0000313|Proteomes:UP000195273}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMR4r {ECO:0000313|EMBL:ARU00788.1,
RC ECO:0000313|Proteomes:UP000195273};
RA Topel M., Pinder M.I.M., Johansson O.N., Kourtchenko O., Godhe A.,
RA Clarke A.K.;
RT "Genome Sequence of Loktanella vestfoldensis Strain SMR4r Isolated from a
RT Culture of the Diatom Skeletonema marinoi.";
RL Submitted (MAY-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}.
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DR EMBL; CP021431; ARU00788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0EBA9; -.
DR STRING; 1122181.GCA_000382265_00390; -.
DR KEGG; lvs:LOKVESSMR4R_01471; -.
DR Proteomes; UP000195273; 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}; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 26..505
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 566..572
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 137
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 908 AA; 100075 MW; 3343DA01D4AA321D CRC64;
MSDTPETPEN NDDLPITRMA HAGPSVTIEH ELKTSYLDYA MSVIVSRAIP DLRDGLKPVH
RRILYGMYEA GNTHDKSYRK SARSVGDVMG KYHPHGDSAI YDALVRMAQD FSMSLPLLDG
QGNFGSMDGD RAAAMRYTEV RMDKPAAYML MDIDKDTVDF QDNYDGKDRE PTVLPARFPN
MLVNGAGGIA VGMATNIPPH NLGEVIDATL ALIDNPDMTS EEMIDYIPGP DFPTGGLILG
RSGARKAYLE GRGSVIVRAK TAVEEIRKDR YAIVINEIPY QVNKSVMIDR IAEAARDKRI
EGIAHVQDES DRNGVRVVVE LKRDATAEVV LNQLFRFTPM QTYFGCNMLA LNGGKPEQLT
LRAFLTAFVD FREEVIARRT AFELRKARER AHILCGLAVA VTNIDEVVAT IRGSADAAAA
RHKLMTRRWP AAAILEYIKL IDDPTHTAND DGTYNLSEAQ ARAILELRLQ RLTQIGVKEV
TDELQELAGK IREYLEILGS RDRILQIIRD ELTEVRDLFA VPRRTQIVDW SGDMDDEDLI
EQEDMVVTVT SGGYIKRTAL ADFRAQRRGG KGLSSMATKE EDVVTTLFVA NTHTQLLFFT
TDGMAYKLKT WRLPLGSRTA KGKAIVNILP IPQGVSVAAI MPVDRPETEW DDLQIVFATS
AGDVRRNALS DFTNVKSNGK IAMKLPDEKT LLVNARICSP EDDVMLVTNS GRAIRFPTTD
VRVFKGRDST GVRGIRLQGD DKVVSMSIIR HFEAEAEERA AYLKMRRAMA GLADDAEVED
EEATPGQISP ERYAEMSAAE NLILTISAKG SGKLSSSHDY PVRGRGGMGV AAMDKAMRGG
PLVTSFPVDM SDQIMLVTST GQSIRVPVEG ISFRSRSAGG VKVFDTGKGE TVVSVAWIAD
QGEDEDEA
//
