ID   GYRA_PECCA              Reviewed;         878 AA.
AC   P41513;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 105.
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};
OS   Pectobacterium carotovorum (Erwinia carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7642123; DOI=10.1016/0378-1119(95)00267-a;
RA   Rosanas A., Barbe J., Gibert I.;
RT   "Cloning and sequencing of the gyrA gene from the plant pathogen Erwinia
RT   carotovora.";
RL   Gene 161:11-14(1995).
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; X80798; CAA56777.1; -; Genomic_DNA.
DR   PIR; S47332; S47332.
DR   AlphaFoldDB; P41513; -.
DR   SMR; P41513; -.
DR   PRIDE; P41513; -.
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; 1.10.268.10; -; 1.
DR   Gene3D; 2.120.10.90; -; 1.
DR   Gene3D; 3.90.199.10; -; 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   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; SSF101904; 1.
DR   SUPFAM; SSF56719; SSF56719; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Topoisomerase.
FT   CHAIN           1..878
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000145233"
FT   REGION          858..878
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           560..566
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        122
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   878 AA;  97589 MW;  6F7D181BADA617E3 CRC64;
     MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMSVLGNDWN
     KPYKKSARVV GDVIGKYHPH GDSAVYETIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM
     RYTEIRMSKI AHELLADLEK ETVDFVPNYD GTEQIPDVMP TRIPNLLVNG SSGIAVGMAT
     NIPPHNLTEV VNGCLAYIDD ENISLEGLME HIKGPDFPTA AIINGRRGIE EAYRTGRGKI
     YIRARAEVEA DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKDKRIEGIS ALRDESDKDG
     MRIVIEIKRD AVGEVVLNNL YSQTQLQTSF GINMVALHQG QPKIMPLKDI LVAFVRHRRE
     VVTRRTIFEL RKARDRAHIL EGLAIALANI DPIIELIRRA ASPAEAKASL IAQAWELGSV
     ATMLERAGDD AARPEWLEPE FGIRDGRYYL TEQQAQAILD LRLQKLTGME HEKLLDEYKE
     LLAEIAELLY ILNSPERLME VIREELEAFK TQYSDERRTE ITANTADINI EDLINQEDVV
     VTLSHQGYVK YQPLSDYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDTI LCFSSRGRLY
     WMKVYQLPEA SRGARGRPIV NLLPLEADER ITAILPVREY EEGRHIFMAT ASGTVKKTAL
     TEFSRHVSGI IAVNLNEGDE LIGVDLTDGS DEAMLFSAEG KVVRFSEQAV RSMGRTATGV
     RGINLQGEDR VVSLIIPRGE GDILTVTQNG FGKRTAVSEY PTKSRATKGV ISIKVSERNG
     KVVGAVQVDA ADQIMMITDA GTLVRTRVSE VSIVGRNTQG VTLIRTAEDE HVVGLQRVAE
     PVEDEELDGV VKVEGEVAED DDAIDDIDGD DDIAEDDE