GYRA_HALL2
ID GYRA_HALL2 Reviewed; 858 AA.
AC P21557; M0GQR6; Q47968;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 2.
DT 03-AUG-2022, entry version 92.
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}; ORFNames=C456_09158;
OS Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)
OS (Haloferax alicantei).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1230452;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 14919 / CCM 7023 / CIP 107410 / JCM 9276 / NCIMB 13854 / Aa 2.2;
RX PubMed=8063095; DOI=10.1016/0378-1119(94)90844-3;
RA Holmes M., Pfeifer F., Dyall-Smith M.;
RT "Improved shuttle vectors for Haloferax volcanii including a dual-
RT resistance plasmid.";
RL Gene 146:117-121(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14919 / CCM 7023 / CIP 107410 / JCM 9276 / NCIMB 13854 / Aa 2.2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
RC STRAIN=DSM 14919 / CCM 7023 / CIP 107410 / JCM 9276 / NCIMB 13854 / Aa 2.2;
RX PubMed=1846146; DOI=10.1128/jb.173.2.642-648.1991;
RA Holmes M.L., Dyall-Smith M.L.;
RT "Mutations in DNA gyrase result in novobiocin resistance in halophilic
RT archaebacteria.";
RL J. Bacteriol. 173:642-648(1991).
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: Mutations in DNA gyrase result in novobiocin resistance
CC in halophilic archaebacteria. {ECO:0000305|PubMed:1846146}.
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; X60178; CAA42740.1; -; Genomic_DNA.
DR EMBL; M38373; AAB09606.1; -; Genomic_DNA.
DR EMBL; AOLH01000015; ELZ74525.1; -; Genomic_DNA.
DR RefSeq; WP_004063238.1; NZ_AOLH01000015.1.
DR AlphaFoldDB; P21557; -.
DR SMR; P21557; -.
DR EnsemblBacteria; ELZ74525; ELZ74525; C456_09158.
DR PATRIC; fig|1230452.3.peg.1757; -.
DR Proteomes; UP000011535; Unassembled WGS sequence.
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:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
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..858
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000145273"
FT REGION 833..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 544..550
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 834..858
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT CONFLICT 105
FT /note="Q -> E (in Ref. 1; CAA42740)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="T -> A (in Ref. 1; CAA42740)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="G -> A (in Ref. 1; CAA42740)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="D -> E (in Ref. 1; CAA42740)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="S -> T (in Ref. 1; CAA42740)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="V -> I (in Ref. 1; CAA42740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 858 AA; 94437 MW; 0D59C30C3C757155 CRC64;
MSSDAPDSFE PGAGIAAEVK NARIEDEMEQ SYIDYAMSVI AGRALPDVRD GLKPVHRRIL
YAMHQAGVTS NSSHRKSSSI VGETMGDYHP HGDSAIYDTL ARMAQDFSMR YPLVDGQGNF
GSVDGDPPAA MRYTEARMSP IAEELLDDID KDTVDFQSNY DDRKQEPTVL PSSFPNLLVN
GSSGIAVGMS TNIPPHNLGE VVDATVELIE NPDATVADLM EHIKGPDFPT GANIVGRNAV
HKAYKTGRGR VRVRADYDVF EEEGRIVINE LPYQENKARL IERIADDVNE GKIEGIRDIR
DESDRDGIRV VIELKRGAMA EVVKNQLLDN HLESTFGVIN LALVDGQPQV LTLKETLEHY
LDHRRDVVRR RSEYELAEAE DRAHILDGRL KALDNIDDVV ETIRNSESRD DAKAALRGEV
EVEVDGEPLP TFDFSEEQAN HIVSMQLGSL TSMEAAEIEA EYEDVQATIE RLETILGDQS
ELDAVIESEL LDIKDEYADD RRTSFVANTG EVTRADLIPE EDVVVVVSED DYIKRMPVSR
FRAQHRGGKG IIGTDLKEGD NVSSVFVTNT HDDLLCFTNH GQVYQLKAYQ VPEMSRTARG
KSAVNLLDFD DGEEITAVVN CDDLEDIEGY LTMVTRNGYI KRTGTDRFQN ILSTGIIATK
LDEGDELVDV EVTDGESDLV IGTERGMSIR FDEDEVRAMG RSARGVRGIK LEGDDVVAGV
AAIDEAHHSW ILTVTENGYG KRTDLDAYRT QSRNGKGLID IKANERNGPV CAINTVGEGD
HLVVMSDEGQ ILRTPVEDIS TVGRNTMGVI VMDLDEGDAV ASVDVIPAAM TTEAEELDDA
DSVEEDAETD AKADADDE
