ID U4TR25_9LACO Unreviewed; 903 AA.
AC U4TR25;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
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:ERL65905.1};
GN ORFNames=L248_1981 {ECO:0000313|EMBL:ERL65905.1};
OS Schleiferilactobacillus shenzhenensis LY-73.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Schleiferilactobacillus.
OX NCBI_TaxID=1231336 {ECO:0000313|EMBL:ERL65905.1, ECO:0000313|Proteomes:UP000030647};
RN [1] {ECO:0000313|Proteomes:UP000030647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY-73 {ECO:0000313|Proteomes:UP000030647};
RX PubMed=24265500;
RA Lin Z., Liu Z., Yang R., Zou Y., Wan D., Chen J., Guo M., Zhao J., Fang C.,
RA Yang R., Liu F.;
RT "Whole-Genome Sequencing of Lactobacillus shenzhenensis Strain LY-73T.";
RL Genome Announc. 1:e00972-e00913(2013).
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; KI271584; ERL65905.1; -; Genomic_DNA.
DR RefSeq; WP_022528848.1; NZ_KI271584.1.
DR AlphaFoldDB; U4TR25; -.
DR STRING; 1231336.L248_1981; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000030647; 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 12..465
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 806..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 527..533
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 863..878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 903 AA; 99146 MW; 22391217BCDA3CA0 CRC64;
MDESQDRRIH TVNLPETMRK SFLDYAMSVI VARALPDVRD GLKPVHRRIL YGMNELGVTP
DKPYKKSARI VGDVMGKYHP HGDSAIYESM VRMAQDFSYR YPLVDGHGNF GSVDGDGAAA
MRYTEARLSK IATEMLRDIN KDTIDFQDNY DGTEREPVVL PSRIPNLLIN GATGIAVGMT
TNIPPHNLGE VISALHILMR NPDATTADLM EALPGPDFPT GGVVMGKSGI RRAYETGRGN
IILRAKVEVQ TEKSGKERII VHEIPYMVNK AKLVERIAEL ARDHRVDGIT TLQDESDREG
MRITIDIRRD TSATVVLNNL YKLTPLQTNF SFNMVAIVDG APKVLTLKQI LVYYLKHQED
VITRRTRFDL RKAEARAHIL AGLRTALDHV DAIVSLLRSA PNGDVAKAQL IDQFDLDDKQ
AQAILDMRMV RLTGLERDKI DSEFNDLQAA IADYKDILAK PERIHEIIYQ ELLDIQKRYG
DKRRTELLVG EVLSIEDEDL IEQEDVVLTL SHNGYIKRLP ASEFKVQNRG GRGIQGMGVH
DDDFIEHLIS SSTHDVLLFF TNQGKVYRAK GYEIPEYSRM AKGIPIINLL GIDSGEQIQT
VINVAENDAA EHYLFFITRD GTVKRTSVRE FANIRSNGLK AINLHDGDEL NNVLLTDGHQ
NIIIGTHDGY SVSFSETAVR NMGRAASGVR GVRLRADDYV IGSDILKPNA EVMVISEKGY
GKRTPTSEYP IKGRGGKGIK TVNVTKKNGP LAGLTVVDGS EDMLLITNTG VLIRFAVTDV
SQTGRAAMGV RVIRLDDDAS VASLAKVAPE EDDGDDGSDA TAPDGGGDTA PAGPAAAGSD
AGDTVSTDTP AAPSADADAP QEGANLSKSQ SNALDELLNR ATEDQDKAEH DDSDDSHHDN
DQE
//
