GYRA_AMICL
ID GYRA_AMICL Reviewed; 817 AA.
AC D5ECW5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=Amico_0252;
OS Aminobacterium colombiense (strain DSM 12261 / ALA-1).
OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae;
OC Aminobacterium.
OX NCBI_TaxID=572547;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12261 / ALA-1;
RX PubMed=21304712; DOI=10.4056/sigs.902116;
RA Chertkov O., Sikorski J., Brambilla E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Tapia R., Goodwin L., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Spring S.,
RA Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Aminobacterium colombiense type strain (ALA-
RT 1).";
RL Stand. Genomic Sci. 2:280-289(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:0000255|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:0000255|HAMAP-
CC 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:0000255|HAMAP-Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR EMBL; CP001997; ADE56397.1; -; Genomic_DNA.
DR RefSeq; WP_013047663.1; NC_014011.1.
DR AlphaFoldDB; D5ECW5; -.
DR SMR; D5ECW5; -.
DR STRING; 572547.Amico_0252; -.
DR EnsemblBacteria; ADE56397; ADE56397; Amico_0252.
DR KEGG; aco:Amico_0252; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_0; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000002366; 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; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 1.
DR Gene3D; 3.90.199.10; -; 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 Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..817
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409820"
FT MOTIF 532..538
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 127
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 817 AA; 91065 MW; 1642743F581D1D1F CRC64;
MEEKKGEPLF GKVVPLPLVE EIKHSYLDYA MSVIVGRALP DARDGLKPVQ RRILYAMMEL
GLRHNTAYKK SARVVGETMG KYHPHGDSAI YDTMVRMAQD FSMRYPLVDG QGNFGSIDGD
PAAAMRYTEA RLYEIGELML ADIDQDTVDW GPNFDESLQE PLCLPAMLPN LLINGSSGIA
VGMATNIPPH NLVEVVDALC YLIDTEPEQV DIGEILFRMP GPDFPTGGLI LGRDGIIDAY
RTGRGKITMR GRTHIEEGKR GKTFIVITEI PYMVNKTNLI ETIAKNVQDK TIDGVMDLRD
ESDREGLRIV IEVNRDTDPN LVLRQLYRRT QLQSTFGVIN LALIDGYPKE LSIEEMLNIF
LNHRRSVVRR RTQFRLEKAE ARAHIVEGLV KALDIIDEVI ALIRGSATTE EAKEGLISKL
DFSEAQAQAI LEMRLQRLTG LEREKLEAEL AQLLSDIERY QTILGNPKVL DSVIKEELLE
VKRRFGNERK TEIIDAVEDV SIEDLIPESD IVVVLSRDGY LRRKDLQEYT LQGRGGKGRK
GTALQEEDEV ALVAVTSTHR DIYLFTSKGR VLALKGYVIP ESKTGRGKLI NRFVALEEGE
RVVTMHGRAV DGAKYAFFIT LRGTAKRLDL SELENLTRAG RRVMGLDEGD EISQIVLTSG
DDHLLIVTAQ GQALRTHESE FRPMGRTARG VRGIRLRKND YVIGCDVVAN GRWPLLLSEN
GFGKRTKYDE FSLRHRGGSG VIVMNLSDRT GLIVGCWSVA EGDEIVAITS RGRMIRLAVS
ESPVLGRTAM GSIMMRLDEG DTVATASVVS TEDGEDD
