GYRA_SHIFL
ID GYRA_SHIFL Reviewed; 875 AA.
AC P0AES5; P09097;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
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};
GN OrderedLocusNames=SF2311, S2444;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43827.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17645.1; -; Genomic_DNA.
DR RefSeq; NP_708120.1; NC_004337.2.
DR RefSeq; WP_001281242.1; NZ_WHSI01000112.1.
DR PDB; 2Y3P; X-ray; 2.62 A; A/B=2-523.
DR PDBsum; 2Y3P; -.
DR AlphaFoldDB; P0AES5; -.
DR SMR; P0AES5; -.
DR STRING; 198214.SF2311; -.
DR PRIDE; P0AES5; -.
DR EnsemblBacteria; AAN43827; AAN43827; SF2311.
DR EnsemblBacteria; AAP17645; AAP17645; S2444.
DR GeneID; 1027274; -.
DR GeneID; 66673880; -.
DR KEGG; sfl:SF2311; -.
DR KEGG; sfx:S2444; -.
DR PATRIC; fig|198214.7.peg.2769; -.
DR HOGENOM; CLU_002977_6_1_6; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR EvolutionaryTrace; P0AES5; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding;
KW Isomerase; Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..875
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145249"
FT REGION 841..875
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 COMPBIAS 845..875
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:0000255|HAMAP-Rule:MF_01897"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:2Y3P"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:2Y3P"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2Y3P"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:2Y3P"
FT TURN 135..139
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 165..169
FT /evidence="ECO:0007829|PDB:2Y3P"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 187..199
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2Y3P"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 270..282
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 327..333
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 347..388
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 403..412
FT /evidence="ECO:0007829|PDB:2Y3P"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 441..449
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 452..460
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 463..466
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 469..492
FT /evidence="ECO:0007829|PDB:2Y3P"
FT HELIX 495..513
FT /evidence="ECO:0007829|PDB:2Y3P"
FT STRAND 519..521
FT /evidence="ECO:0007829|PDB:2Y3P"
SQ SEQUENCE 875 AA; 96964 MW; 3FD5BD52A5969069 CRC64;
MSDLAREITP VNIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN
KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM
RYTEIRLAKI AHELMADLEK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT
NIPPHNLTEV INGCLAYIDD EDISIEGLME HIPGPDFPTA AIINGRRGIE EAYRTGRGKV
YIRARAEVEV DAKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRVEGIS ALRDESDKDG
MRIVIEVKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMNLKDI IAAFVRHRRE
VVTRRTIFEL RKARDRAHIL EALAVALANI DPIIELIRHA PTPAEAKTAL VANPWQLGNV
AAMLERAGDD AARPEWLEPE FGVRDGLYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE
LLDQIAELLR ILGSADRLME VIREELELVR EQFGDKRRTE ITANSADINL EDLITQEDVV
VTLSHQGYVK YQPLSEYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDHI LCFSSRGRVY
SMKVYQLPEA TRGARGRPIV NLLPLEQDER ITAILPVTEF EEGVKVFMAT ANGTVKKTVL
TEFNRLRTAG KVAIKLVDGD ELIGVDLTSG EDEVMLFSAE GKVVRFKESS VRAMGCNTTG
VRGIRLGEGD KVVSLIVPRG DGAILTATQN GYGKRTAVAE YPTKSRATKG VISIKVTERN
GLVVGAVQVD DCDQIMMITD AGTLVRTRVS EISIVGRNTQ GVILIRTAED ENVVGLQRVA
EPVDEEDLDT IDGSAAEGDD EIAPEVDVDD EPEEE
