ID   GYRA_BORHD              Reviewed;         810 AA.
AC   B2S0D7;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=BH0435;
OS   Borrelia hermsii (strain HS1 / DAH).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX   NCBI_TaxID=314723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HS1 / DAH;
RA   Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA   Schwan T.G.;
RT   "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT   comparative analysis of two agents of endemic N. America relapsing fever.";
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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; CP000048; AAX16943.1; -; Genomic_DNA.
DR   RefSeq; WP_012422199.1; NC_010673.1.
DR   AlphaFoldDB; B2S0D7; -.
DR   SMR; B2S0D7; -.
DR   KEGG; bhr:BH0435; -.
DR   HOGENOM; CLU_002977_4_1_12; -.
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   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..810
FT                   /note="DNA gyrase subunit A"
FT                   /id="PRO_0000409821"
FT   MOTIF           529..535
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT   ACT_SITE        124
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   810 AA;  91510 MW;  519F55E956EDB253 CRC64;
     MVTEEDKEQI LNIKIEDEVK TSYLNYAMSV IVSRALPDVR DGLKPVHRRI LYSMHEMGLR
     ADKAFKKAGR IVGDVLGKYH PHGDQSIYEA LVRLAQDFSL RYPIVIGQGN FGSIDGDPPA
     AMRYTEARMA RVAEELVRDI DKQTVDFRAN YDDSLLEPEV LPAAFPFLLV NGSSGIAVGM
     ATNMAPHNLK EICDAIVYML DHDSVSVYDL IEIVKGPDFP TYAEIIYNES LIKAYTTGKG
     SVVIRARYHI EEKFEDHIAI IITQIPYAVN KSSLLMKIAF LIKEEKLEGV SDIRDESDRE
     GIRIVLEIKK GFDPHVVMNL LYEYTELRKN FSINNLALVN GIPKQLNLKE LISAFIEHRK
     EIVRRRVEFD LKRAREKAHI LEGLNIALRN IDRVIEIIRF ARLVKDAKEC IIKEFNLSEI
     QANSILDMKL QKLTSIETEK LEEEFKILLA LIKDYEDILN SPERVVNIVR EEIINLSLKF
     GDERRTKIIY DEEVLKTSMS DLMQRENVIV ILTKQGFIKR ILQDEYKLQG IGGKGLGSFD
     LQDRDQVNIT LCVNTHDFLF MISNEGKLYV INAYGIKDTS RTSKGQNVRE LINLGETEEI
     LAIKNCNELS VDNYLLITTA NGKIARIETE GFKTVKARGV IVIKLDDNDF VTSAEIVSKN
     EKIICISKKG NAFAFNSDNI RLTHRGTQGV SGMKVREGDV LIKALAVKQG SHLLVVSENG
     YGKRLEISKV TDLKRGATGY TCYKKSDEKA GEVVDAITVV QDDEILLVSK GAKVLRTLVD
     KISEQGKDAR GMQVLSLDED KLISVSKFIK