GYRA_CAMJE
ID GYRA_CAMJE Reviewed; 863 AA.
AC Q03470; Q0P9M5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=Cj1027c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UA580;
RX PubMed=8384814; DOI=10.1128/aac.37.3.457;
RA Wang Y., Huang W.M., Taylor D.E.;
RT "Cloning and nucleotide sequence of the Campylobacter jejuni gyrA gene and
RT characterization of quinolone resistance mutations.";
RL Antimicrob. Agents Chemother. 37:457-463(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; L04566; AAA23028.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL35145.1; -; Genomic_DNA.
DR PIR; A48902; A48902.
DR RefSeq; WP_002857904.1; NC_002163.1.
DR RefSeq; YP_002344422.1; NC_002163.1.
DR AlphaFoldDB; Q03470; -.
DR SMR; Q03470; -.
DR IntAct; Q03470; 23.
DR STRING; 192222.Cj1027c; -.
DR PaxDb; Q03470; -.
DR PRIDE; Q03470; -.
DR EnsemblBacteria; CAL35145; CAL35145; Cj1027c.
DR GeneID; 905319; -.
DR KEGG; cje:Cj1027c; -.
DR PATRIC; fig|192222.6.peg.1009; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_7; -.
DR OMA; THHWLLF; -.
DR Proteomes; UP000000799; 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 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Cytoplasm; DNA-binding; Isomerase;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1..863
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145227"
FT MOTIF 527..533
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 125
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT VARIANT 70
FT /note="A -> T (in strain: UA67; confers resistance to
FT nalidixic acid and ciprofloxacin)"
FT VARIANT 86
FT /note="T -> I (in strain: UA580R1, UA536, UA543 and UA549;
FT confers resistance to nalidixic acid and ciprofloxacin)"
FT VARIANT 90
FT /note="D -> N (in strain: UA580R3; confers resistance to
FT nalidixic acid and ciprofloxacin)"
SQ SEQUENCE 863 AA; 96974 MW; CB8C577F8D6EAF8B CRC64;
MENIFSKDSD IELVDIENSI KSSYLDYSMS VIIGRALPDA RDGLKPVHRR ILYAMQNDEA
KSRTDFVKSA RIVGAVIGRY HPHGDTAVYD ALVRMAQDFS MRYPSITGQG NFGSIDGDSA
AAMRYTEAKM SKLSHELLKD IDKDTVDFVP NYDGSESEPD VLPSRVPNLL LNGSSGIAVG
MATNIPPHSL NELIDGLLYL LDNKDASLEE IMQFIKGPDF PTGGIIYGKK GIIEAYRTGR
GRVKVRAKTH IEKKTNKDVI VIDELPYQTN KARLIEQIAE LVKERQIEGI SEVRDESNKE
GIRVVIELKR EAMSEIVLNN LFKSTTMEST FGVIMLAIHN KEPKIFSLLE LLNLFLTHRK
TVIIRRTIFE LQKARARAHI LEGLKIALDN IDEVIALIKN SSDNNTARDS LVAKFGLSEL
QANAILDMKL GRLTGLEREK IENELAELMK EIARLEEILK SETLLENLIR DELKEIRSKF
DVPRITQIED DYDDIDIEDL IPNENMVVTI THRGYIKRVP SKQYEKQKRG GKGKLAVTTY
DDDFIESFFT ANTHDTLMFV TDRGQLYWLK VYKIPEGSRT AKGKAVVNLI NLQAEEKIMA
IIPTTDFDES KSLCFFTKNG IVKRTNLSEY QNIRSVGVRA INLDENDELV TAIIVQRDED
EIFATGGEEN LENQEIENLD DENLENEESV STQGKMLFAV TKKGMCIKFP LAKVREIGRV
SRGVTAIKFK EKNDELVGAV VIENDEQEIL SISAKGIGKR TNAGEYRLQS RGGKGVICMK
LTEKTKDLIS VVIVDETMDL MALTSSGKMI RVDMQSIRKA GRNTSGVIVV NVENDEVVSI
AKCPKEENDE DELSDENFGL DLQ
