ID A0A1I3DW59_9FLAO Unreviewed; 881 AA.
AC A0A1I3DW59;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA gyrase subunit A {ECO:0000256|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000256|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN ORFNames=SAMN05443292_0734 {ECO:0000313|EMBL:SFH90873.1};
OS Halpernia frigidisoli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Halpernia.
OX NCBI_TaxID=1125876 {ECO:0000313|EMBL:SFH90873.1, ECO:0000313|Proteomes:UP000198931};
RN [1] {ECO:0000313|EMBL:SFH90873.1, ECO:0000313|Proteomes:UP000198931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26000 {ECO:0000313|EMBL:SFH90873.1,
RC ECO:0000313|Proteomes:UP000198931};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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:0000256|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:0000256|ARBA:ARBA00000185,
CC ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01897}.
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DR EMBL; FOQT01000001; SFH90873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3DW59; -.
DR STRING; 1125876.SAMN05443292_0734; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000198931; 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: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; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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 NCBIfam; TIGR01063; gyrA; 1.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01897};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01897}; Reference proteome {ECO:0000313|Proteomes:UP000198931};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..466
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 862..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..881
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 881 AA; 98940 MW; 56B0F89024316A4E CRC64;
MHKEGERLIP INIVDEMKSS YIDYSMSVIV SRALPDVRDG LKPVHRRVLY GMYGLNVFSN
RKHLKSARIV GDVLGKYHPH GDSSVYDAMV RMAQPWSLRY PQVDGQGNFG SMDGDPPAAM
RYTEARLKKI SDDILSDLDK DTVDFQFNFD DSLTEPKVMP SRIPNLLVNG TSGIAVGMAT
NMAPHNLTES INGICAYIDN NEITIDELMQ HIIAPDFPTG GIIYGYDGVR EALHTGRGRI
VLRAKINFEE VHNRNAIIVT EVPYQVNKAD MIARTADLVK DDKIPGIYEI RDESDRNGLR
VVYELKNDAI PNVVLNLLYK YTALQTSFSC NNIALVGGRP VQLNVKDLIR HFVDHRHEVV
VRRTTFEIKK AKERAHILEG FMKVIGTQDS LDTAIRIIRN SSNPADAKQG LIDEFELSDI
QAQAILDMRL ARLTGMELDK IRAEYDEIMA LINDLQDILD NEPRRFEIIK EELLEVKEKY
GDERRTEIDY SGGEMSIEDI IPNESVVLTI SHAGYVKRTL LSEYKVQSRG GVGNRAATTR
DADFLEYIVT ATNHQYLMFF TEKGKCYWLR VFEIPEGSKT SKGRAVQNLI NIEPDDKIKA
YIRTNDLKDK EYIQKMNVVM ITKNGTIKKT SLEAYSRPRV NGINAIEIRE DDVLLGAKLT
DGNSQIMIAT KNGKCIRFPE EKARAVGRGS IGVRGISLTD GDEVIGMIAV NDLENDTVLV
VSEKGYGKRT AVEDYRITNR GGKGVITLNI TEKTGNLIAI QSVTDEDGLM IINKSGVAIR
MNMDNMRVMG RNTQGVRMIN LRKDDEIAAI AKVEMDKEVA EEIDEDAEIV IDSNNPETSN
IPETGDNVLN IGDPEVLKQI EEEEAQKNAD LEDESEEEDN N
//
