ID A0A2M6VE34_9BURK Unreviewed; 892 AA.
AC A0A2M6VE34;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=B9Z41_10430 {ECO:0000313|EMBL:PIT76702.1};
OS Limnohabitans sp. JirII-31.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1977908 {ECO:0000313|EMBL:PIT76702.1, ECO:0000313|Proteomes:UP000228925};
RN [1] {ECO:0000313|EMBL:PIT76702.1, ECO:0000313|Proteomes:UP000228925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JirII-31 {ECO:0000313|EMBL:PIT76702.1,
RC ECO:0000313|Proteomes:UP000228925};
RA Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA Simek K., Ghai R.;
RT "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL Submitted (APR-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: 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:PIT76702.1}.
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DR EMBL; NESA01000007; PIT76702.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M6VE34; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000228925; 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:UP000228925};
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 868..892
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 892 AA; 98994 MW; B90A2D4C02652F7B CRC64;
MTQFAKETLP ISLEEEMRRS YLDYAMSVIV GRALPDARDG LKPVHRRVLF AMHELNNDWN
RPYKKSARIV GDVIGKYHPH GDSAVYDTIV RMAQDFSLRH MLVDGQGNFG SVDGDNAAAM
RYTEIRLSKI AHEMLADIDK ETVDFGPNYD GSEKEPLVLP SRIPNLLVNG SSGIAVGMAT
NIPPHNLNEV VDACLHMLRH PQASIDELME IIPAPDFPTA GIIYGMSGVR DGYRTGRGRV
VMRAKCHFED IDRGQRQSII VDELPYQVNK KTLQERMAEL VHEKKIEDIS HIQDESDKSG
MRLVIELKRG AVPEVVLNNL YKQTQLQDTF GINMVALIDG QPKLCNLKDL ISVFLQHRRE
VVTRRTIFTL RKARERGHVL EGLAVALANI DEFIAIIRNA PTPPVAKAEL MTRPWDSKLV
REMLTRSRAD GGVINADDYR PDGLEKEFGM GNDGLYRLSD TQAQEILQMR LQRLTGLEQD
KIVNEYKDVM AEIDDLLDIL AKPERVSTII GDELNVVKQE FGQTKLGARR SVIEHNAQDL
GTEDLITPTD MVVTLSHSGY IKSQPLSEYR AQKRGGRGKQ ATATKEDDWI DQLFIANTHD
YILCFSNRGR LYWLKVWEVP AGSRGSRGRP IVNMFPLQEG EKINVVLALT GEARTFPENQ
FVFMATSMGT VKKTSLDEFN NPRKGGIIAV NLDDGDFLVG AALTDGKHDV MLFSDGGKAV
RFDENDVRPL GRSARGVRGM MIEDGQSVIA MLVSEQEDPN APADAVRASV LTATENGYGK
RTSITEYTRH GRGTKGMIAI QQSERNGKVV AATLVQADDE IMLITDTGVL VRTRVSEIRE
LGRATQGVTL IGLDAGAKLS GLQRIVENDA NANDSEGTED GQAGDTSTPN EA
//
