ID A0A1S1V4B6_9FIRM Unreviewed; 808 AA.
AC A0A1S1V4B6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ECO:0000313|EMBL:OHW61294.1};
GN ORFNames=EUAN_23310 {ECO:0000313|EMBL:OHW61294.1};
OS Andreesenia angusta.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Gottschalkiaceae;
OC Andreesenia.
OX NCBI_TaxID=39480 {ECO:0000313|EMBL:OHW61294.1, ECO:0000313|Proteomes:UP000180254};
RN [1] {ECO:0000313|EMBL:OHW61294.1, ECO:0000313|Proteomes:UP000180254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1989 {ECO:0000313|EMBL:OHW61294.1,
RC ECO:0000313|Proteomes:UP000180254};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Eubacterium angustum.";
RL Submitted (SEP-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: 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:OHW61294.1}.
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DR EMBL; MKIE01000017; OHW61294.1; -; Genomic_DNA.
DR RefSeq; WP_071064667.1; NZ_MKIE01000017.1.
DR AlphaFoldDB; A0A1S1V4B6; -.
DR STRING; 39480.EUAN_23310; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000180254; 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:UP000180254};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 525..531
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 808 AA; 91095 MW; 6ADDB0CD054023C0 CRC64;
MSEEMNNLKK IDIEQEMKKS YLDYAMSVIV SRALPDVRDG LKPVHRRIIY AMNELSLQPE
KPHRKSARIV GDVLGKYHPH GDTAVYDAMV RLAQEFSTRY LLVDGHGNFG SVDGDSAAAM
RYTEARMGKI TTEMLRDIEK ETIDYRPNFD ETLDEPKVLP SRFPNLLANG SSGIAVGMAT
SIPPHNLKEI INGIVELIEN PEVEVEDILK HIKGPDFPTG AMIMGKDGLS EAYRTGRGKV
TVRAVSNIEV NEKGRSSIIF TEIPYQVNKA REIEKIASLV RDKKIEGISD LRDESDRDGM
RIVVEVKKDA NPNVILNKLY KYTQLQNTFS IIMIALVDDR PKLLNLKEIM QHYLSHQHNV
IVRRTKYELK KAESRAHILE GLKIALDRID EVIKLIRGSK IAQEAKDGLI EKFGLSEIQA
QAILDMRLQR LTGLERGKIE DEYKNIILEI AKFKEILSSD ELIYKIIKDE LLEIKEKYGD
KRRTRIVPAE DELDMEDLID EEDVVINLTH MGYIKRMPED TYKTQRRGGR GISGITTRDE
DFVSDLFTTS THDNLLFFTN QGRAYCLKAY DIPEAKRQAK GTAIINLLQL NPGEKVNAVI
PIRDFSKESY LVMVTDHGVI KKIDLEQLKS IRKTGIIAIT LKDGDELISV RKTSGEDQLI
AVTSYGLAIM FEETDVRAMG RTAAGVKAMT LKEGDKIVGV DLVEESKDLL VISENGYGKR
TPLEDYRLQK RGGKGIKTYN VKDVTGNLIS AKVVSHEDEV MINSTMGTII RLNVGDISNM
GRTTQGVRLM KMQKDDKVSS VAKIVAEE
//
