GYRA_CAMFE
ID GYRA_CAMFE Reviewed; 862 AA.
AC P47235;
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 Campylobacter fetus.
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=196;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27374 / UA60;
RX PubMed=9056011; DOI=10.1128/aac.41.3.665;
RA Taylor D.E., Chau A.S.;
RT "Cloning and nucleotide sequence of the gyrA gene from Campylobacter fetus
RT subsp. fetus ATCC 27374 and characterization of ciprofloxacin-resistant
RT laboratory and clinical isolates.";
RL Antimicrob. Agents Chemother. 41:665-671(1997).
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; U25640; AAA67068.1; -; Genomic_DNA.
DR RefSeq; WP_011732215.1; NZ_RBHV01000015.1.
DR AlphaFoldDB; P47235; -.
DR SMR; P47235; -.
DR STRING; 983328.AFGH01000033_gene812; -.
DR GeneID; 61065280; -.
DR OMA; THHWLLF; -.
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; Topoisomerase.
FT CHAIN 1..862
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145226"
FT REGION 843..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 528..534
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 848..862
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 862 AA; 95821 MW; E450D81809A10C35 CRC64;
MEENIFSSNQ DIDAIDVEDS IKASYLDYSM SVIIGRALPD ARDGLKPVHR RILYAMNDLG
VGSRSPYKKS ARIVGDVIGK YHPHGDTAVY DALVRMAQNF SMRVPAVDGQ GNFGSVDGDG
AAAMRYTEAR MTVLAEELLR DLDKDTVDFI PNYDDSLSEP DVLPARVPNL LLNGSSGIAV
GMATNIPPHS LDELVNGLLT LLDDKEVGLE DIMTHIKGPD FPTGGIIFGK KGIIEAYKTG
RGRIKLRAKT HIEKKPNKDV IVVDELPYQV NKAKLHADIA DLVKEKLIDG ISEVRDESDR
DGIRLVIELK RDAMSEIVLN NLFKSTQMEV TFGVIMLAIN NKEPKVFSLL ELLKLFLNHR
KTVIIRRTIF ELQKARARAH ILEGLKIALD NIDAVINLIK TSADTNSARD GLMAKFGLSE
LQSNAILDMR LSKLTGLERE KLEAELKEIL ELIEKLDAIL KSETLIENII RDELLEIKSK
FKCPRITDIV DDYDDIDVED LIPNENMVVT ITHRGYIKRV PSKSYEKQKR GGKGKVAVTT
YDDDFIESFF TCMSHDTLMF VTDRGQLYWL KVYKIPEGSR TAKGKAVVNL ISLQADEKIK
AIIPTTDFDE SKSLAFFTKN GIVKRTNLSE FKNIRSIGVK AINLDDNDEL VTVVIANSEP
DESYDDSFED GEGVSNLQTI SEDNSENSLE SGKMLFAVTK KGMCIKFALN KVRQIGRVSR
GVTAIRFKEN LDEVVGAVVI ENDSQEILSV SQKGIGKRTT ADEYRLQSRG GKGVICMKLT
PKTKDLVGVV MVDEEMDLMA LTSSGKMIRV DMQSIRKAGR NTSGVIVVNV DGDEVVSIAR
CPKEESDDDD IVADDTQEQD ME
