ID A1R0S8_PAEAT Unreviewed; 889 AA.
AC A1R0S8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 127.
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:ABM07057.1};
GN OrderedLocusNames=AAur_0007 {ECO:0000313|EMBL:ABM07057.1};
OS Paenarthrobacter aurescens (strain TC1).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Paenarthrobacter.
OX NCBI_TaxID=290340 {ECO:0000313|EMBL:ABM07057.1, ECO:0000313|Proteomes:UP000000637};
RN [1] {ECO:0000313|EMBL:ABM07057.1, ECO:0000313|Proteomes:UP000000637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC1 {ECO:0000313|EMBL:ABM07057.1,
RC ECO:0000313|Proteomes:UP000000637};
RX PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V., Khouri H.,
RA Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT "Secrets of soil survival revealed by the genome sequence of Arthrobacter
RT aurescens TC1.";
RL PLoS Genet. 2:2094-2106(2006).
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}.
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DR EMBL; CP000474; ABM07057.1; -; Genomic_DNA.
DR AlphaFoldDB; A1R0S8; -.
DR SMR; A1R0S8; -.
DR STRING; 290340.AAur_0007; -.
DR KEGG; aau:AAur_0007; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_11; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000000637; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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 31..488
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 856..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..501
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 142
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 889 AA; 98699 MW; 53C71B889C26F522 CRC64;
MSDETPEVPE PNDVEDVVLE GDVLTDRVEQ VDLQTEMQRS YLDYAMAVIV GRALPDVRDG
LKPVHRRVLY AMFDGGYRPD RSFNKCARVV GDVMGTYHPH GDMAIYDALV RLIQDWTMRY
PLALGQGNFG SPGNDGAAAP RYTETKMAQL AMEMVRDIDE ETVDFQDNYD GKNQEPTILP
ARFPNLLVNG SSGIAVGMAT NIPPHNLREV AEGVQWALDN PTATREELLE ALLLRIKGPD
FPTGATILGH KGIEDAYRTG RGSITMRAVV NVEELQGRTC LVVTELPYQA NPDNLAIKIA
ELVKDGKIQG IADLRDETSG RTGQRLVIVL KRDAVAKVVL NNLYKHTQLQ DNFSANMLAI
VDGVPRTLSL DAFIRHWVAH QMDVIARRTR YRLRKAEEEA HILRALLKAL DMLDEVIALI
RASNTTEAAR EGLMELLEID ELQARAILDM QLRRLAALER QKIQDRHSEL EAMIQEYNAI
LASEERQRQI ISEELAEIVA KHGDDRRTHI LMGFDGDMSM EDLIPEEEMV VTITRGGYVK
RTRSDNYRSQ QRGGKGIKGA QLRGDDVVEH FFVTTTHHWL LFFTNLGRVY RAKAYELAEA
GRDAKGQHVA NLLAFQPDEH IAQVLDLRDY QQAPYLVLAT KNGLVKKTRL EDYDTNRTAG
VIAINLRDED ELVSAQLVSE TDDLLLVSRK GQSIRFTATD DALRPMGRAT SGVTGMKFRE
DDELLAADVV QDGSFVFIVT EGGYAKRTAV DEYRLQGRGG LGIKVAKLAE DRGDLVGALI
VQEEDEVLVV MEGGKVVRSA VTGVPAKGRD TMGVIFAKPD KNDRIIEVAR NSERGLEVEE
SEDGLDDDVT LAANDGASEA TVTAETENDA DPEFETGAEL NEDNTGGNE
//
