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Database: UniProt
Entry: B3ESJ9_AMOA5
LinkDB: B3ESJ9_AMOA5
Original site: B3ESJ9_AMOA5 
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}.
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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
//
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