ID R9KUU1_9ACTN Unreviewed; 931 AA.
AC R9KUU1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=C811_01923 {ECO:0000313|EMBL:EOS50294.1};
OS Adlercreutzia caecimuris B7.
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Adlercreutzia.
OX NCBI_TaxID=1235794 {ECO:0000313|EMBL:EOS50294.1, ECO:0000313|Proteomes:UP000014204};
RN [1] {ECO:0000313|EMBL:EOS50294.1, ECO:0000313|Proteomes:UP000014204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B7 {ECO:0000313|EMBL:EOS50294.1,
RC ECO:0000313|Proteomes:UP000014204};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterorhabdus caecimuris B7.";
RL Submitted (APR-2013) 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS50294.1}.
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DR EMBL; ASSY01000009; EOS50294.1; -; Genomic_DNA.
DR RefSeq; WP_016310107.1; NZ_KE159646.1.
DR AlphaFoldDB; R9KUU1; -.
DR STRING; 1235794.C811_01923; -.
DR GeneID; 82191325; -.
DR PATRIC; fig|1235794.3.peg.1896; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_2_11; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000014204; 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}; 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:UP000014204};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 91..544
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 509..536
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 605..611
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 1..46
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..931
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 202
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 931 AA; 103200 MW; 4D6CAD4C4B94336A CRC64;
MADFEDENFD ADEQSGVEAA EEDALYLAEE VDTDDEGDED AEIASASSTL DEEHAVSEEE
RARSMMVDMP NPHGSIIEGA NGGEGTTVRA AFLGKEMQTS FLEYSMSVIV SRALPDVRDG
LKPVHRRILY AMNESGYTPS KPHMKSARTV GDVIGKYHPH GDSAVYDTMV RLAQPFSLRL
PLIDGHGNFG SIDGDSAAAM RYTEARLDKP AMELLRDLDK ETVDFQPNYD ESLQEPTVLP
ARFPNLLVNG SNGIAVGMAT NIPPHNLGET IDATCLMIDN PECTTEELMA VMPGPDFPTG
GLIMGKKGIL DAYETGHGNM TIRAKCEIEE KKNGRSSIVV KEIPYQVNRK RLLEKLGELV
RDKKLPEISN IHDAADRKGI DIIIDLKSNA IPQVVLNKLY KHTQLQVGFG ANMLALVNGT
PRVLSLKEIL HYYIEHQKDV VTRRTRYELA KAEEREHILE GYIIALDNID EVIQIIRSSQ
TDKEAAARLT ERFGLSEKQT NAILEMRLRR LTGLEREKIE EELAELREKI AYYKRILSDE
SLLKQVIKDE LLEIKKKYGN PRRTRITGEA KDIEVEDLIA EENMVVTMTK AGYIKRLPVS
TYRQQKRGGK GMQGVNLKDA DFVEHLFVAS THSYMLFFST KGKVYRLKVY EIPEASRHAR
GTAIVNLLPL EKGESISAVI ATKDFPAEEF LMFATAQGNV KKTSMDQYDR TRRDGLIAIN
LKDDDELISV KRVAKGEKVI MVSSAGKAIL WDESEARAMG RGTMGVRGMN VPADAHVLGM
EIARPGTDLF VITEKGYGKR TKIEEYPEHH RGGQGVYTIT MTHKKGLLAV MKIVGADDEI
MIVSEEGVIV RTPVKGISEL GRSTQGVKVM NVADKDKVCA VAISSTGKKK AKKEGPADEN
QLDLLDEEST DGSLAIDDID GDEGDVEAAE E
//
