GYRA_HAEIN
ID GYRA_HAEIN Reviewed; 880 AA.
AC P43700;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 136.
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=HI_1264;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(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}.
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; L42023; AAC22917.1; -; Genomic_DNA.
DR PIR; E64113; E64113.
DR RefSeq; NP_439419.1; NC_000907.1.
DR RefSeq; WP_005694321.1; NC_000907.1.
DR AlphaFoldDB; P43700; -.
DR SMR; P43700; -.
DR STRING; 71421.HI_1264; -.
DR DrugBank; DB06771; Besifloxacin.
DR DrugBank; DB00827; Cinoxacin.
DR DrugBank; DB00537; Ciprofloxacin.
DR DrugBank; DB00467; Enoxacin.
DR DrugBank; DB09047; Finafloxacin.
DR DrugBank; DB04576; Fleroxacin.
DR DrugBank; DB01155; Gemifloxacin.
DR DrugBank; DB00365; Grepafloxacin.
DR DrugBank; DB01137; Levofloxacin.
DR DrugBank; DB00978; Lomefloxacin.
DR DrugBank; DB00218; Moxifloxacin.
DR DrugBank; DB01059; Norfloxacin.
DR DrugBank; DB01165; Ofloxacin.
DR DrugBank; DB12924; Ozenoxacin.
DR DrugBank; DB00487; Pefloxacin.
DR DrugBank; DB01208; Sparfloxacin.
DR DrugBank; DB01405; Temafloxacin.
DR DrugBank; DB00685; Trovafloxacin.
DR DrugCentral; P43700; -.
DR EnsemblBacteria; AAC22917; AAC22917; HI_1264.
DR KEGG; hin:HI_1264; -.
DR PATRIC; fig|71421.8.peg.1316; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_6; -.
DR OMA; THHWLLF; -.
DR PhylomeDB; P43700; -.
DR BioCyc; HINF71421:G1GJ1-1292-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009330; C:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0006265; P:DNA topological change; IBA:GO_Central.
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 Reference proteome; Topoisomerase.
FT CHAIN 1..880
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145235"
FT MOTIF 557..563
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 880 AA; 97818 MW; 0B2E9DD34155A322 CRC64;
MTDSIQSSIT PVNIEEELKS SYLDYAMSVI VGRALPDVRD GLKPVHRRVL FSMDREGNTA
NKKYVKSARV VGDVIGKYHP HGDSAVYDTI VRMAQPFSLR YMLVDGQGNF GSIDGDAPAA
MRYTEVRMQK ITQALLTDLD KETVNFSPNY DGELMIPDVL PTRIPALLAN GSSGIAVGMA
TNIPPHNLNE VLNGCLAYID KNEITIDELM QHIPGPDFPT AALINGRKGI EEAYRTGRGK
VYVRARATVE TNEKGREQII VSELPYQVNK AKLVEKIAEL IREKKIEGIS NITDLSNKEG
IRIEIDIKRD AVGEVVLNHL YSLTQMQVTF GINMVALDHG QPRLFNLKEI IEAFVLHRRE
VVTRRSIFEL RKARERTHIL EGLAVARSNI DEMIAIIRNS KNREEAATSI SSRSWTLHSD
IINLLDASAR PDELEENLGI QGEQYYLSPA QVNAILELRL HRLTGIAFEE VIKEYEELLV
KIADLLHILS SAERLMEVIR EELEEVKAQF GDDRLTEITA ASGDIDLEDL IAQEDVVVTL
SHEGYVKYQP LTDYEAQRRG GKGKSATKMK EEDFIEKLLV ANTHDTILCF SSRGRLYWLK
VYQLPQASRG ARGRPIVNIL PLQENERITA ILPVSAYEED KFVVMATAGG IVKKIALTEF
SRPRSNGIIA LNLRDEDELI GVDITDGSNE IMLFSSQGRV VRFAENAVRA MGRLATGVRG
IKLALTNDIS DDESAVEIED ISDDNAEASL DLNIDKVVSL VVPKGEGAIL TATQNGYGKR
TQLSEYPTKS RNTKGVISIK VSERNGKVVA ATQVEETDQI MLITDAGTLV RTRVSEVSIV
GRNTQGVRLI RTADDEHVVS LERVCDADED DSLEESSSEE
