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Entry: C5B7G2_EDWI9
LinkDB: C5B7G2_EDWI9
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ID   C5B7G2_EDWI9            Unreviewed;       878 AA.
AC   C5B7G2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 97.
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   OrderedLocusNames=NT01EI_2630 {ECO:0000313|EMBL:ACR69798.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR69798.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACR69798.1, ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|EMBL:ACR69798.1,
RC   ECO:0000313|Proteomes:UP000001485};
RX   PubMed=22247535; DOI=10.1128/JB.06522-11;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA   Lawrence M.L.;
RT   "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT   a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL   J. Bacteriol. 194:740-741(2012).
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 topoisomerase GyrA/ParC subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01897}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263}.
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DR   EMBL; CP001600; ACR69798.1; -; Genomic_DNA.
DR   RefSeq; WP_015871906.1; NC_012779.2.
DR   AlphaFoldDB; C5B7G2; -.
DR   STRING; 67780.B6E78_05165; -.
DR   GeneID; 69539529; -.
DR   KEGG; eic:NT01EI_2630; -.
DR   PATRIC; fig|634503.3.peg.2344; -.
DR   HOGENOM; CLU_002977_6_1_6; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000001485; 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}; 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..499
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          844..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           560..566
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   COMPBIAS        845..878
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        122
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   878 AA;  96945 MW;  6A5CFBE62A49F1AF CRC64;
     MSDLAREITP VNIEEELKNS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMNVLGNDWN
     KPYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM
     RYTEVRMAKI AHELLADLDK ETVDYVPNYD GTEQIPDVLP TKVPNLLVNG SAGIAVGMAT
     NIPPHNLTEV INGCLAYIDD ENITIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKI
     YVRARAEIEV DDKNSRETIV VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG
     MRIVIEVKRD AVGEVVLNNL YSQTQMQVSF GINMVALHQG QPKLLTLKEC LEAFVRHRRE
     VVTRRTIFEL RKARGRAHIL EGLAIALVNI DPIIELIRRA PTPAEAKAAL VSQAWALGNV
     AAMLARAGDD AARPEWLEPQ YGIRDGHYHL TEQQAQAILD LRLQKLTGLE HEKLLDEYKA
     LLEQIAALIF ILQSPERLME VIREELIAIR EQFGDARRTE ITANTADINI EDLIEQEDVV
     VTLSHQGYVK YQPLSDYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDTI LCFSSRGRMY
     WMKVYQLPEA SRGARGRPII NLLPLEADER ITAILPVREY AEGVNVFMAT ASGTVKKTAL
     AEFSRPRAAG IIAVNLNDGD ELIGVDLTDG NDEVMLFSAA GKVVRFKEDA VRAMGRTATG
     VRGIKLAGDD RVVSLIVPHG EGAILTVTQN GYGKRSSVAE YPTKSRATQG VISIKVTERN
     GSVVGAVQVE DSDQIMMITD AGTLVRTRVS EVSIVGRNTQ GVILIRTAED EHVVGLQRVV
     EPVDDEDLDS IDGSAAEGDD EIVPEVESDD DAAEDDAE
//
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