ID A0A124JZJ6_9SPHN Unreviewed; 910 AA.
AC A0A124JZJ6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=AQZ49_01310 {ECO:0000313|EMBL:KUR80700.1};
OS Novosphingobium sp. FSW06-99.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1739113 {ECO:0000313|EMBL:KUR80700.1, ECO:0000313|Proteomes:UP000061032};
RN [1] {ECO:0000313|EMBL:KUR80700.1, ECO:0000313|Proteomes:UP000061032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSW06-99 {ECO:0000313|EMBL:KUR80700.1,
RC ECO:0000313|Proteomes:UP000061032};
RA Ruckert C., Winkler A., Glaeser J., Grossart H.-P., Kalinowski J.,
RA Glaeser S.;
RT "Draft genome sequence of Novosphingobium sp. FSW06-99 (=LMG 27919), a
RT Novosphingobium acidiphilum related species isolated from a surface water
RT sample of the southwest basin of Lake Grosse Fuchskuhle.";
RL Submitted (OCT-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}.
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:KUR80700.1}.
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DR EMBL; LLZQ01000001; KUR80700.1; -; Genomic_DNA.
DR RefSeq; WP_067611675.1; NZ_KQ954251.1.
DR AlphaFoldDB; A0A124JZJ6; -.
DR STRING; 1739113.AQZ49_01310; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000061032; 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:UP000061032};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 22..501
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 884..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 562..568
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 133
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 910 AA; 100323 MW; 96D357600F041611 CRC64;
MSDDNTPIDP TNPTGVPEFQ RIDIVDEMKS SYLDYAMSVI VSRALPDVRD GLKPVHRRIL
WTSHENGFTA GKPYRKSARI VGDCMGKYHP HGDSAIYDAL ARMTQDWSMR LPLIDGQGNF
GSMDPDPPAS MRYTEARLAK VADALLGDIE KDTVDFQPNY DGAENEPQVL PARFPNLLVN
GAGGIAVGMA TNIPPHNLGE VIDGCFAYMD NPLISIDELI RIIPGPDFPT APLILGTAGA
RKAYTEGRGS IIMRARHAIE DARGRRSIVL TSIPYQVGKS NLVEKIAEAA KDKRIEGVAD
IRDESNREGV RVVIDLKRDA TPEVVLNQLW RNTPAQSNFP ANMLAIRGGR PETLSLKDII
ECFVRFREEV ITRRTKFELM KARDRAHILL GLVIAVTNLD EVVRIIRGSA NPGIAREALL
TREWPIQEIA SYIKLVEAIE DDELEDTLTY RLSETQVRAI LDLRLHRLTA LGRDEIGGEL
ETLAKAIAEY LSILADREKL YGVMRDELMA VRTQFATPRL SEITAPADGI EDEDLIERED
MVVTITLDGY IKRTPLSTFR AQNRGGKGRS GMATKDEDAV GTMFVASTHT PVLFFSTAGK
VYRLKVWRLP EGGAATRGRP VVNLLPALDQ GETIAAVLAL PEDEAEWGKL DVMFATALGN
VRRNAMDAFA NIPSNGKYAM RFEEGDEDRL IGVALLSEGD DVLLASRQGK AIRFAADDVR
EFQSRTSTGV RGMLLKDGDE VISLSILHRT SLRDQDERDE YLRFAPWKAE REGEPGIDPA
RFAELAEGEQ FILTVCANGY GKLSSAYEYR RTGRGGQGIT NIDNIERNGP VVASFPAVQA
DQLMLVTDQA KLIRLPLTTL RVIGRGSAGV RLFNVSDSEH VVSAARLDEP EEEETTEATA
SDDGVDTAGE
//
