ID A0A0G0MQ44_YANXG Unreviewed; 819 AA.
AC A0A0G0MQ44;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=UT29_C0001G0046 {ECO:0000313|EMBL:KKR02566.1};
OS Yanofskybacteria sp. (strain GW2011_GWA1_39_13).
OC Bacteria; Candidatus Yanofskybacteria.
OX NCBI_TaxID=1619019 {ECO:0000313|EMBL:KKR02566.1, ECO:0000313|Proteomes:UP000034845};
RN [1] {ECO:0000313|EMBL:KKR02566.1, ECO:0000313|Proteomes:UP000034845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GW2011_GWA1_39_13 {ECO:0000313|Proteomes:UP000034845};
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKR02566.1}.
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DR EMBL; LBWF01000001; KKR02566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MQ44; -.
DR PATRIC; fig|1619019.3.peg.47; -.
DR Proteomes; UP000034845; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 19..473
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 535..541
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 130
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 819 AA; 90808 MW; 552C6279683A231A CRC64;
MSSKHFLFKH GMGTGIKQRE IVQEMQKAYL EYAMSVIVAR ALPDVRDGLK PVHRRILYSM
HEMGLRPTAK TQKSAKVVGY VLGNYHPHGD TAAYDSMVRM AQDFSLRYPL VNGQGNFGSI
DGDSPAAYRY TEARLAPISE QLLADIDKQT VDFTDNFDGT MQEPTVLPTR IPNLLINGSM
GIAVGMATNI PPHNLTEILD ALVYLTDNKD ADLSELTQFV KGPDFPTGGV IYNEKDINTA
YATGRGPIIM RGQADITENK KGYQIIISEI PYQVNKAELI IKMADLVKEK KIEGIKDIRD
ESDREGMRIA IDLKQDAFPK KVLNQLFKYT ELQKSFHFNM LALVDGGTQP QILGLKGLLE
KFIEHRREVV VRRTKFELQK AKDRAHILEG LKKALDHIDE IIKIIRASAS KEDAFNNLIK
KFKFSDKQAT AILEMKLQAL AGLERKKLED ELKEKMELIA YLESLLASPK KLLGVIKDEF
KEIREKYGDE RRTKVVKSAL REIGEDELMP EEDSLFMITH SGYIKRMQPD GLKSQKRGGK
GLIGMATKEE DVISQFFMAN THDSLLFFTN SGKVFQTKGY EVPESSRQSK GKAIVNFLNV
SPSEIITAVV PIPKEQKGGY LFMATANGVI KKVDADSFSQ VRSNGMIAIK LKGNDELGWV
LSTTGNDQVM LVTSGGNAIR FKEKDVRPMG RGASGVIGVR MDKDEKVVGA DVVPSGVEKG
LKILVVMGNG YGKRTDLKFY KIQGRGGRGI MTAKITPKTG KLVSAHITSE ENKELIAVSK
KGVVIRTSID SVSVLGRATQ GVRVMRVEAG DGLASVVVV
//
