ID A0A0P0LGN8_9BURK Unreviewed; 894 AA.
AC A0A0P0LGN8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:ALK88076.1};
GN ORFNames=L63ED372_00854 {ECO:0000313|EMBL:ALK88076.1};
OS Limnohabitans sp. 63ED37-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK88076.1, ECO:0000313|Proteomes:UP000059510};
RN [1] {ECO:0000313|EMBL:ALK88076.1, ECO:0000313|Proteomes:UP000059510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK88076.1,
RC ECO:0000313|Proteomes:UP000059510};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-2015) 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}.
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DR EMBL; CP011774; ALK88076.1; -; Genomic_DNA.
DR RefSeq; WP_062403735.1; NZ_CP011774.1.
DR AlphaFoldDB; A0A0P0LGN8; -.
DR STRING; 1678128.L63ED372_00854; -.
DR KEGG; lih:L63ED372_00854; -.
DR PATRIC; fig|1678128.3.peg.848; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000059510; 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; 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:UP000059510};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..507
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 872..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 572..578
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 894 AA; 99155 MW; 24C4D0CB45503142 CRC64;
MTQFAKETLP ISLEEEMRRS YLDYAMSVIV GRALPDARDG LKPVHRRVLF AMHELNNDWN
RPYKKSARIV GDVIGKYHPH GDQSVYDTIV RMAQDFSMRH MLVDGQGNFG SVDGDNAAAM
RYTEIRLAKI AHEMLADIDK ETVDFGPNYD GSEKEPLVLP SRLPNLLING SGGIAVGMAT
NIPPHNLNEV VDACLHLLRN PEASIDELME IVPAPDFPTG AIIYGMTGVK EGYRTGRGRV
VMRAKCHFED IDKGQRQCIV VDELPYQVNK KTLQERMAEL VHEKKIEDIS HIQDESDKSG
MRLVIELKRG AVPEVVLNNL FKQTQLQDTF GMNMVALIDG QPKLCNLKDL IQVFLQHRRE
VVTRRTVFEL RKARDRGHVL EGLAVALANI DDFIAIIRGA PTPPVAKAEL MTRAWDSQMV
RTMLTRARDD GSVVNADDYR PEGLEREYGL GQDGLYRLSD TQAQEILQMR LQRLTGLEQD
KIVAEYKEVM SEIEDLLDIL AKPERVSTII GDELGTVRQE FGQTKIGARR SEIEHSAQDL
STEDLITPTD MVVTLSHSGY IKSQPLSEYR AQKRGGRGKQ AAATKEDDWI DQLFIANTHD
YLLCFSNRGR LYWLKVWEVP AGSRGSRGRP IVNMFPLQEG EKINVVLALT GEARTFPDNQ
YVFMATSMGT VKKTSLDEFS NPRKGGIIAV NLDEGDFLIG AALTDGKHDV MLFSDGGKAV
RFDENDVRPL GRSARGVRGM MIEDHQSVIA MLVSEQEDPA AAADDTVARA SVLTATENGY
GKRTNISEYT RHGRGTKGMI AIQQSERNGK VVAATLVQAE DEIMLITDTG VLVRTRVSEI
REMGRATQGV TLIGLDEGAK LSGLQRIVEN DANVSEGEAG DADAAADDSA PAAE
//
