ID W6M8C4_9GAMM Unreviewed; 869 AA.
AC W6M8C4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:CDI04221.1};
GN ORFNames=BN873_890127 {ECO:0000313|EMBL:CDI04221.1};
OS Candidatus Competibacter denitrificans Run_A_D11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Competibacteraceae; Competibacter.
OX NCBI_TaxID=1400863 {ECO:0000313|EMBL:CDI04221.1, ECO:0000313|Proteomes:UP000035760};
RN [1] {ECO:0000313|EMBL:CDI04221.1, ECO:0000313|Proteomes:UP000035760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI04221.1,
RC ECO:0000313|Proteomes:UP000035760};
RA McIlroy S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDI04221.1, ECO:0000313|Proteomes:UP000035760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Run_A_D11 {ECO:0000313|EMBL:CDI04221.1,
RC ECO:0000313|Proteomes:UP000035760};
RA McIlroy S.J., Albertsen M., Andresen E.K., Saunders A.M., Kristiansen R.,
RA Stokholm-Bjerregaard M., Nielsen K.L., Nielsen P.H.;
RT "Candidatus Competibacter-lineage genomes retrieved from metagenomes reveal
RT functional metabolic diversity.";
RL Submitted (FEB-2014) 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:CDI04221.1}.
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DR EMBL; CBTJ020000101; CDI04221.1; -; Genomic_DNA.
DR RefSeq; WP_048676122.1; NZ_CBTJ020000101.1.
DR AlphaFoldDB; W6M8C4; -.
DR STRING; 1400863.BN873_890127; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000035760; 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:UP000035760};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..499
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 839..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 560..566
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 845..869
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 869 AA; 95953 MW; 600AAB8F6BD8871A CRC64;
MTEIAKEILP VNLEDEMRQS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMSELGNDWN
KPYKKSARVV GDVIGKYHPH GDTAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDAPAAM
RYTEVRMSRI AHELLADLDK ETVDFAPNYD ESEREPAVFP TRLPNLLVNG SSGIAVGMAT
NIPPHNLGEV VDACVALIDE PNLSIGQLMR HIPGPDFPTA ALINGAHGIR DAYETGRGRV
QMRARTEIET DEARGRQAII VTELPYQVNK ARLIEKIAEL VKDKKIEGIT ELRDESDKDG
MRIYIELRRN ENAEVVLNNL FLHTPLQCVF GVNMVALVDG QPRLLNLKQV LEAFLSHRRE
VVVRRTVFEL RKARERAHIV EGLAVALANL DSLIALIRAA TDPAAAKAAL LERVWVPGLV
TELLDQSGAL TSRPDDLSAE YGLVEGGYRL SPVQAQAILD LRLHRLTGLE QRKLLDEYQE
LLSRIQALLA ILTQPQRLTA VIRAELQELR AQYADARRTV IQPDESNLNL EDLITDETMV
VTLSHAGYVK SQPLSLYRAQ KRGGRGRAAT TVREEDFVDK LFIASTHDTV LCFSNRGKVY
WKKVYELPQA GRTARGKPIV NLLPLEEGER INAVLSVREF GDDHYVFFAT TNGTVKKTPL
SEYSRPRPSG IIAIDLRDGD QLVNVELTDG QRDVMLFSDA GKAVRFTETD VRDTGRSAYG
VRGIRLGEGQ KVIALIVVDE GTVLTVTENG FGKRTPAAEY ARHGRGGQGV IAIQTSERNG
RVIGAVQVEN DHEIMLISDG GTLVRTRVGE ISVVGRNAQG VKLISLQGEE KLAGVEKIES
MGELESNGDE TEEDAGSVPD DGENGEGVE
//
