ID A0A239SNT7_9BURK Unreviewed; 873 AA.
AC A0A239SNT7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:SNU86929.1};
GN ORFNames=SAMEA4530655_03578 {ECO:0000313|EMBL:SNU86929.1};
OS Pandoraea sputorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Pandoraea.
OX NCBI_TaxID=93222 {ECO:0000313|EMBL:SNU86929.1, ECO:0000313|Proteomes:UP000215126};
RN [1] {ECO:0000313|EMBL:SNU86929.1, ECO:0000313|Proteomes:UP000215126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13161 {ECO:0000313|EMBL:SNU86929.1,
RC ECO:0000313|Proteomes:UP000215126};
RG Pathogen Informatics;
RL Submitted (JUN-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT906435; SNU86929.1; -; Genomic_DNA.
DR RefSeq; WP_039400090.1; NZ_LT906435.1.
DR AlphaFoldDB; A0A239SNT7; -.
DR STRING; 93222.NA29_21970; -.
DR KEGG; pspu:NA29_21970; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000215126; Chromosome 1.
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 11..506
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 567..573
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 873 AA; 96706 MW; EFB190C15262FEA5 CRC64;
MDQFAKETLP ISLEEEMRRS YLDYAMSVIV GRALPDVRDG LKPVHRRALF AMHELNNDWN
RAYKKSARIV GDVIGKYHPH GDASVYDTIV RMAQPFSLRY MLVDGQGNFG SVDGDNAAAM
RYTEVRMAKI GHELLADIDK ETVDFGPNYD GSEKEPLILP ARIPNLLLNG SSGIAVGMAT
NIPPHNLNEV VEGCLYVLKN PEATVDELIE IIPAPDFPTA GIIYGISGVR EGYRTGRGRV
VMRAKTHFED IDRGQRVAII VDELPYQVNK RSLLERIAEL VNEKRLEGIS DIRDESDKSG
MRVVIELKRG EVPEVVLNNL YKHTQLQDTF GMNMVALVDG QPKLLNLREM LVHFLAHRRE
VITRRTVYEL RRARERGHVL EGLAVALANI DDFIAIIKAA PTPPIAKAAL MEKSWDSSVV
REMLARAETE TQGGLAAYRP EGLDVAVGVQ PDGLYRLSET QAQEILQMRL QRLTGLEQDK
IVSEYKEVMA QIADLLDILA SPPRVTAIIS EELTAVRAEF GDARRSTIEH NATELDTEDL
ITPQDMVVTL SHSGYIKSMP LSEYRAQKRG GRGKQAAATK DDDWIDTLFI ANTHDTILCF
SNRGRVYWIK VYEVPQGSRN SRGRPIVNMF PLQDGEKINV VLPVKEYTED RFVFMATSLG
TVKKTPLAAF SRPLKKGIIA VNLDDGDVLI GAAITDGAHD VMLFSDAGKA VRFDENDVRP
MGREARGVRG MQLEDGQTVI ALLVAENEQQ SVLTATVNGY GKRTSITEYT RHGRGTKGMI
AIQTSERNGR VVAATLVEPD DEIMLITTGG VLIRTRVSEI REMGRATQGV TLISLDEGTT
LSGLQRIVET DAEVAENGDA QGDDEAPEAD VTE
//
