ID B3ESJ9_AMOA5 Unreviewed; 816 AA.
AC B3ESJ9;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 94.
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 OrderedLocusNames=Aasi_0828 {ECO:0000313|EMBL:ACE06201.1};
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471 {ECO:0000313|EMBL:ACE06201.1, ECO:0000313|Proteomes:UP000001227};
RN [1] {ECO:0000313|EMBL:ACE06201.1, ECO:0000313|Proteomes:UP000001227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2 {ECO:0000313|EMBL:ACE06201.1,
RC ECO:0000313|Proteomes:UP000001227};
RX PubMed=20023027; DOI=10.1128/JB.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
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 topoisomerase GyrA/ParC subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
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; CP001102; ACE06201.1; -; Genomic_DNA.
DR RefSeq; WP_012472970.1; NC_010830.1.
DR AlphaFoldDB; B3ESJ9; -.
DR STRING; 452471.Aasi_0828; -.
DR KEGG; aas:Aasi_0828; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_10; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000001227; Chromosome.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000001227};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 12..465
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 465..492
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 526..532
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 816 AA; 91254 MW; 5A4B78891EF4041F CRC64;
MAIEPQENII PINIVDEMRT AYIDYSMSVI IARALPDVRD GLKPVHRRVL YGMHELGVTH
NKPFKKSARI VGEVLGKYHP HGDASVYDAM VRMAQDWSLR YPLVQGQGNF GSIDGDGPAA
MRYTEARLAR TAEEMLADLN KDTVDFQTNF DDSLQEPTVL PAKLPQLLIN GSSGIAVGMA
TNMPPHNLTE VIEGIIAYIN NNDITIEELM QYIQGPDFPT RGIIYGSQGI REAYRTGRGK
VLMRAKATIE TTPTGKEQII VTEIPYMVNK AMLIERTAQL VNEKKIEGIS DIRDESDKDG
LRIVYDLKRD AIGQVVLNNL YKNTSLQFSF GVNNVALVAG KPQTLNLKEL IQHFVAHRHE
VLLRKTKYEL NQAQKRLHIL EGYLIALDNL DAIISLIRSS RDAEAAKQGL IQTYQLSEQQ
AKAILELRLQ RLTGMERDKI LQEHRETTQL IERLQLILSD RDLQMTLIKN ELAELKEQYG
DARRTVIEHN TDDITLEDMI AEEDMVITIS QQGYIKRTPL SEYRIQNRGG VGARSTATKE
DDYITHLFVA STHQYLLIFT TLGKVFWKKV YTLPEGSKSS KGRAIQNLIP IAPGDQVQSV
IKVRNLKDET YVNSRYILMC TVQGVIKKTP LDAYINPRTN GIQAIKINEG DRLLTVKLTK
GDNHVIIALR SGRAIHFHER DVRSMGRVST GVRGITLAGP EDRVVGMVTV YKPDIELLVV
AEKGVGKRSA VADYRITKRG GKGVKTLNIT EKTGALAAIE AVTDADELLI INTSGIAIRI
EVSTLRIMGR NTQGVRLIRL NEGDAITSIA KITENL
//