ID A0A2C6C5P4_9BACT Unreviewed; 854 AA.
AC A0A2C6C5P4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CEQ90_01285 {ECO:0000313|EMBL:PHI21949.1};
OS Lewinellaceae bacterium SD302.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae.
OX NCBI_TaxID=2014804 {ECO:0000313|EMBL:PHI21949.1, ECO:0000313|Proteomes:UP000223945};
RN [1] {ECO:0000313|EMBL:PHI21949.1, ECO:0000313|Proteomes:UP000223945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SD302 {ECO:0000313|EMBL:PHI21949.1,
RC ECO:0000313|Proteomes:UP000223945};
RA Wang K.;
RT "The draft genome sequence of Lewinellaceae bacterium SD302.";
RL Submitted (JUL-2017) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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:PHI21949.1}.
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DR EMBL; PDLQ01000001; PHI21949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6C5P4; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000223945; 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:UP000223945};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 10..493
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 465..506
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 854 AA; 95896 MW; E8A79E19F6E7FE94 CRC64;
MSPEQRIIPV NIEEQMKSAY IDYSMSVIVS RALPDVRDGL KPVHRRVLFG MQELGISYRS
AHKKSARIVG EVLGKYHPHG DSSVYGTMVR MAQDWSLRYP LVDGQGNFGS MDGDSPAAMR
YTEARLERIS DDILSDLGKD TVDFQLNFDD TLKEPTVLPT KIPNLLVNGA SGIAVGMATN
MLPHNLTEVI DGVTATVDNP EITIDELMQF IKAPDFPTGG IIYGIDGVRE AFMTGRGRVV
LRGRAEIIVD NNDRETIIIS EIPYQVNKAN LVAKIAELVN EKKIEGISDV RDESDRDGLR
VVVEVKRDAM ASIVLSYLYK YTPLQSSYGV NNVALVNGRP MTLNLKDMVE EFIKFRLEVI
TRRTQFELNK ALNRAHILIG LIIALDYLDE IIALIRASSN PEEARLGLMA GDFIEDKQAF
WSKFGDLVKE VQTEELITEE GNVLSEAQAK AILEMRLQKL TGLELDKIRE EYQEIRELID
RLRAILESET LRRDIVKDEL REIRERFGDD RRSEISLDTS DISITDMIAD EDVVITISNL
GYIKRTPVTE YRTQSRGGRG SRGSKTRNAD FIEHMFVASN HNYLLLFTEQ GRCHWLRAYE
IPEASKDSGG RVIQNILAIP KDDQVRAYIV IEDLTDEEFL NNNYIVFATR RGMVKKTLVE
AYSRPRTNGI NAITINEGDQ LLEAKLTNGK SRIILGTSQG QAIQFEEEKV RSVGRTASGV
RGVSLAGDHD RVVGMVTLDP ELEQDQDKSI MVVSEQGMGK RTHFEEYRLT NRGGKGVRTM
KVSDKTGELI AIKGVTEADQ LMITNRSGIV IRMKVSDLRE MGRATQGVRV IRVDKGDSIS
DVAVVRDVDD EEEE
//
