ID GYRA_LAWIP Reviewed; 820 AA.
AC Q1MQ89;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=LI0784;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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:0000255|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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR EMBL; AM180252; CAJ54838.1; -; Genomic_DNA.
DR RefSeq; WP_011526867.1; NC_008011.1.
DR AlphaFoldDB; Q1MQ89; -.
DR SMR; Q1MQ89; -.
DR STRING; 363253.LI0784; -.
DR KEGG; lip:LI0784; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_7; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000002430; 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.
DR PROSITE; PS52040; TOPO_IIA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..820
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409827"
FT DOMAIN 31..496
FT /note="Topo IIA-type catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01384"
FT MOTIF 523..529
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 119
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 820 AA; 91735 MW; 065A898744EAADA8 CRC64;
MSQTEHHISI EQEMRKSYLE YSLSVIIGRA IPDVRDGLKP VHRRILFAQQ ELGNSYTRPP
KKCARIVGDV IGKYHPHGDS AVYDALVRMA QDFSMRDPLE EGQGNFGSID GDAPAAMRYT
EVRMSRLASE FLSDIDKETV DFRPNYDNSL EEPIVLPTKV PNLLLNGSSG IAVGMATNIP
PHNLGELCNA LLKIIDDPDV PIDNLLNIIH GPDFPTGGFI YVGQGLYDAY TKGRGTVKVR
GKVEIEERKK GAQSIVIREI PFGLNKSSLV EKIAILVNER KIDGIADLRD ESDRKGIRVV
IELKKGVIPE IIINALYKFT PLETSFGINM LAVVDNRPQL LTIKSALTYF LDHRREVIVR
RTRFELNKAE ARLHILIGLI HALDHIDEVV NLIRSSSTPA EAKIRLIERF SLSEIQAQSI
LDMRLQRLTG LEREKLEEEM HELQTKIAWY ESILGDTKIL WGVIRDEVTG IKEMYTTPRR
TEVIRETLTN IEIEDLIPDD DVVITLSRRG YIKRTNLAIY QQQRRGGKGV AGLHTSEDDF
VQEFITTTNH QFLLLFTNKG RMHQLKVHQV PEGSRTAKGT HIANIVPLEK EEWVTTILTV
REFSDNKFFL FATRKGMVKR SSASYYARSR RTGLLAVGLR EDDELIMVKE VTNNDFIVLA
TAEGFAIRFS CEDVRNMGRG AAGVKGIALR PGDSVVACLI LQEKQDTPAI MTVSNLGYGK
RTSIDLYRVQ TRGGKGIINF KVTQKTGLVI GAKPVSDDNA LVLLTSTNKI IRMSVDEVRS
AGRATMGVRL VKLDDGAYVV GFDTVDGTVD DSCDDATINT
//
