ID A0A2A3VPL5_9GAMM Unreviewed; 903 AA.
AC A0A2A3VPL5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=CMZ82_00915 {ECO:0000313|EMBL:PBS14066.1};
OS Xanthomonadaceae bacterium NML93-0792.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae.
OX NCBI_TaxID=2032566 {ECO:0000313|EMBL:PBS14066.1, ECO:0000313|Proteomes:UP000218683};
RN [1] {ECO:0000313|EMBL:PBS14066.1, ECO:0000313|Proteomes:UP000218683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML93-0792 {ECO:0000313|EMBL:PBS14066.1,
RC ECO:0000313|Proteomes:UP000218683};
RA Bernier A.-M., Bernard K.;
RT "Clinical and environmental strains of Xanthomonadaceae.";
RL Submitted (SEP-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: 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:PBS14066.1}.
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DR EMBL; NTJH01000001; PBS14066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3VPL5; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000218683; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..498
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 870..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 559..565
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 903 AA; 99415 MW; 9825A0EC194D5141 CRC64;
MVDSAKEIIP VNLEDEMRRS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMNELGAHSN
KPYFKSARIV GDVIGKYHPH GDQSVYDTLV RMAQPFSLRY MLVDGQGNFG SVDGDSAAAM
RYTEARMARL THELMADIDK ETVDFQPNYD EKELEPSVMP TRFPNLLVNG SAGIAVGMAT
NIPPHNLNEV VDALIALIDN PEIDIDGLME YIPGPDFPTA GIINGVGGIH LAYRTGRGRV
RMRARAEIEV ADNGREAIAV TEIPYQVNKA RLIEKIAELV KEKRLEGISE LRDESDKDGM
RIYIEVKRGE SAEVVLNNLY SQTQMESVFG INMVALVDGR PQLLNLKQIL EAFVRHRREV
VTRRTIFELR KARNRAHILE GLTVALANID EMIELIKTSA NPNEARERML ARTWAPGLVA
SLLGAAGADA SRPEDLPDGV GLIEGMYQLT ETQAQQILEM RLHRLTGLEQ DRLTEEYKQL
LEVIRGLIEI LEDPDVLLEV IRTELRNVKE EFGDERRSEI RASEEDLDIL DLIAPEDVVV
TLSHSGYAKR QPVSAYRAQK RGGRGRNAAS TKDEDFIEQL WLVNTHDTLL TFTSAGRVFW
LPVHQLPDAG PNARGRPIIN WIPLEADEKV QAVVPVREYV DGHYVFFATR AGTVKKTPLT
EFAYRLARGK IAIRLDDGDA LVGVALTDGD KDVLLFASNG KTVRFAEDRV RSMGRTAGGV
RGIRLAAGEQ VVSLIVADSA GVTVEDEAAD EAGDDAAVET GDEIAVVEAG AGDDIPYILT
ATENGYGKRT PLSEYPCKGR GTQGVIGIQT TERNGPLVGA VLLRNHDEVL LISNGGTLVR
TRASEIARVG RNTQGVTLMR LSKDERLQGI ERVDGSIDDD AADDGVEPPP VEMPSTDAPT
TSP
//
