GYRA_LEPBA
ID GYRA_LEPBA Reviewed; 843 AA.
AC B0S912;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=LBF_0009;
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / Ames;
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
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; CP000777; ABZ92556.1; -; Genomic_DNA.
DR RefSeq; WP_012387044.1; NC_010842.1.
DR AlphaFoldDB; B0S912; -.
DR SMR; B0S912; -.
DR KEGG; lbf:LBF_0009; -.
DR HOGENOM; CLU_002977_6_1_12; -.
DR OMA; THHWLLF; -.
DR BioCyc; LBIF355278:LBF_RS00045-MON; -.
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; 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 Topoisomerase.
FT CHAIN 1..843
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409828"
FT MOTIF 555..561
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 149
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 843 AA; 93818 MW; 16DD3CB95E8BB29A CRC64;
MTEQNGQENE SNKTLALNLS GRPDVAGALK AGVRVIPVEI EDQMKEAYLD YAMSVIVGRA
LPDVRDGLKP VHRRVLHAMN ERAWRSDRPY VKSAKIVGEV IGNYHPHGDS AVYETMVRMA
QTFSMRETLI DGQGNFGSVD GDNAAAYRYT EARLTKLAEE LLKDIEKNTV SFSPNFDDTR
QQPDVLPANF PNILVNGSTG IAVGMATNIP PHNLKEAVNA VIALIQNPDI TLPELMKILP
GPDFPTGGTI IGGEGLYQAY ATGKGSIRIR SKVDIIENNK GREIIVIHEI PYQVNKKNML
EKIGDLVNEK IIEGISEILD LSDRKGIRVE IHVKKDANAQ VILNQLFKLT QLQVSYGITM
LAILDNRPKI FSLKEILKSY AEHRREVVVK RTEFDLDKAQ KRAHILEGLR IALENIDEVI
RIIRASKDVR EAQSSLMATF SLSELQADAI LEMRLQRLTS LEVQKIIDEL EQVRILIADL
EDILSKPDRV KSIICDELGK VSQSFGNTRT TEISLESLES STFNAEDLIA DEEVVVQLSE
DMFIKRLPMD TFRRQKRGGK GVQGISTKRE DFVKKLSSAM THDNLMLFSN KGRAFLLKVY
ELPIATKEAR GKSLKAVINL NDDEIITSLF TFRNFDESYL LMVTREGFVK KIQLDEFTNT
KKSGIIAIGL RDGDELIDVI ANPNNYDVFI GSKNGLAIRM NLNELRSQGR TASGVTAMKL
EDDDSIAGIT KVEPNTNLFC ISENGFGKRT DFEEFSTKGR GGKGMTYLKI GEKNGRAVGI
SSVKEEDELL VITQSGMAIR VEVKTISMVG RSAMGVKVVN TKDEDFVKDF AVVRESDSDS
AES
