GYRA_AERSA
ID GYRA_AERSA Reviewed; 922 AA.
AC P48369;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, 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};
OS Aeromonas salmonicida.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=645;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=2148/89;
RA Oppegaard H.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-179.
RC STRAIN=ATCC 14174 / NBRC 12659 / NCIMB 833;
RX PubMed=7840589; DOI=10.1128/aac.38.10.2460;
RA Oppegaard H., Sorum H.;
RT "gyrA mutations in quinolone-resistant isolates of the fish pathogen
RT Aeromonas salmonicida.";
RL Antimicrob. Agents Chemother. 38:2460-2464(1994).
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; L47978; AAB41037.1; -; Genomic_DNA.
DR EMBL; L42453; AAA87239.1; -; Genomic_DNA.
DR PIR; I39542; I39542.
DR AlphaFoldDB; P48369; -.
DR SMR; P48369; -.
DR STRING; 1233098.GCA_000315855_04900; -.
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; 7.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 2.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Topoisomerase.
FT CHAIN 1..922
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145218"
FT REGION 715..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 561..567
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 723..746
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"
SQ SEQUENCE 922 AA; 101334 MW; 8894965DC4217077 CRC64;
MSDLAREITP INIEEELKSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMNELGNDWN
KPYKKSARVV GDVIGKYHPH GDSAVYDTIV RLAQDFSMRY MLVDGQGNFG SVDGDSAAAM
RYTEVRMARI SHELLADLDK ETVDWVPNYD GTEMIPAVMP TKVPNLLVNG SSGIAVGMAW
NIPPHNLTEI VNGCLALIEN GNLTIDELMT YITGPDFPTG AIINGRAGIV QAYRTGRGSV
YVRAKAEVEV DDKTSRETII IVHELPYQVN KARLIEKIAE LVKEKKVEGI SALRDESDKD
ACRIVIEIKR GESGEIVLNN LYKHTQLQTT FGINMVALDN NQPKVMNLKD ILDAFLLHRR
EVVTRRTVFE LRKARDRAHI LEGLAVALAN IDPIIELIRH SDTPADAKAK LVARGWELGN
VAAMLEKAGD DAARPEWLEP EFGIREGQYF LTEQQAQAIL DLRLHKLTGL EHGKILEEYQ
SLLDLIAELL FILASPERLM EVIRDELLAV REQYGDERPP EISASSAEIN IEDLITPEDV
VVTLSHQGYV KYQPITDYEA QRRGGRGKSA TRIKEENFVE RLLVANTHDT ILCFSTRGKV
YWLKVYQLPE ASRGARGRPI INLLPLEEGE RITAILPVKE YADDKYVFFA TADGTVKKTS
LSAFSRPLSS GIRAINLKEG DELIGVDITD GSNEIMLFSD AGKVVRFNEG SAAPMQPMLM
SSDDVDGDDE SVIDAGNDDD GSDNGEGSES TESKGTFKGV RPMGRTAGGV RGIRLLNGDK
VVSLIVPRGE GAILTATENG YGKGTALTEY PTKSRGTQGV RSIKVDEDGK VSIDQVDDTD
QIMLITNGGT LVRTRVSEVS IIGRNTGGVR LIRTGEDETV VGLQRIAESY EEENDVMAID
GEVSEGTDTA PDAGSAAADP EE
