ID A0A023D2C7_ACIMT Unreviewed; 927 AA.
AC A0A023D2C7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=Amme_018_007 {ECO:0000313|EMBL:GAJ28282.1};
OS Acidomonas methanolica NBRC 104435.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidomonas.
OX NCBI_TaxID=1231351 {ECO:0000313|EMBL:GAJ28282.1, ECO:0000313|Proteomes:UP000019760};
RN [1] {ECO:0000313|Proteomes:UP000019760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB58 {ECO:0000313|Proteomes:UP000019760};
RX PubMed=24330138; DOI=10.1111/1574-6968.12357;
RA Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA Matsushita K., Azuma Y.;
RT "Draft Genomic DNA Sequence of the Facultatively Methylotrophic Bacterium
RT Acidomonas methanolica type strain MB58.";
RL FEMS Microbiol. Lett. 351:9-13(2014).
RN [2] {ECO:0000313|EMBL:GAJ28282.1, ECO:0000313|Proteomes:UP000019760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB58 {ECO:0000313|EMBL:GAJ28282.1,
RC ECO:0000313|Proteomes:UP000019760};
RA Higashiura N., Hadano H., Hirakawa H., Matsutani M., Takabe S.,
RA Matsushita K., Azuma Y.;
RT "Draft genomic DNA sequence of the facultatively methylotrophic bacterium
RT Acidomonas methanolica type strain MB58.";
RL FEMS Microbiol. Lett. 351:9-13(2014).
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:GAJ28282.1}.
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DR EMBL; BAND01000018; GAJ28282.1; -; Genomic_DNA.
DR RefSeq; WP_042056725.1; NZ_BJVB01000002.1.
DR AlphaFoldDB; A0A023D2C7; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000019760; 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:UP000019760};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 16..494
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 762..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 555..561
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 127
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 927 AA; 102191 MW; 50BC89D918695CD4 CRC64;
MTDLNDPKDP LDHLPVTIEE EMRSSYLAYA MSVIVSRALP DVRDGLKPVH RRILYAMRES
GFTADKPYRK SARAVGDVMG KYHPHGDSSI YDAMVRMAQP WSMRVPLIDG QGNFGSVDGD
SPAAMRYTEA RLAKSASFLL DDIDRGTVDF QPNYDESEDE PRVLPAAFPN LLVNGASGIA
VGMATNIPTH NPGEIIDATL AMIADPEITL DELMKIVPGP DFPTGGIIMG RRGIRLAFET
GRGSIPVRAR AEIEDIRKDR KAIVVTEIPY QVNKATLQEK IADLVRAKEI EGISDIRDES
DRSGMRIVIE LKRDATPDVV LNQLYRFTQL QTSFAVNCLA LDDGRPRTMG LRDVLEAFIR
FREEVILRRA RFDLNKARDR GHLLVGLVLA VANIDEVIAL IRAAPDAAAA REALMTRQWN
AADVVPLLAL IHDEGNVVED GKVRLTEAQA RGILELRLQR LTGLEREKIQ AELDEVAAKI
NDLLEIIGSH VRRMEVMREE LTAVRAALTS PRMTEISDAL GDQSDESLVE PGQMVVTITR
DGFIKRTPLD IFRAQNRGGR GRTAAGRRGD DVVVRSFNAH THQWVLFFSS GGKAYREKVW
RLPEASPTAK GRALVNLLPE LGADSITAVL PLPQDETLWE PLHLVFATAS GNVRRNRLSD
FRNIRASGLI AMKLDEGDRL IGVATCREGQ DVFLATRKAR CVRFQITDDT LRVFAGRDSS
GVRGIRLQPG DEVNSLCVLN HVDATVEERA AYLKAANAKR RALQQDEETE EPEEELAEDS
EAVATVGDLA PERFEEMERQ EEILLTVTDA GFGRRSSAYD YRVSGRGGLG IANMTLANPR
RGKEVVATLP VLEGEDIMMV TDVGRLVRTP VGQIRVMARQ ASGVTLCRVG DEERVAAVFP
VMESEGEEGD DDVAAPDDPT PADSAGE
//
