ID A0A2N8Z919_9VIBR Unreviewed; 885 AA.
AC A0A2N8Z919;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:SON48390.1};
GN ORFNames=VTAP4600_A0411 {ECO:0000313|EMBL:SON48390.1};
OS Vibrio tapetis subsp. tapetis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1671868 {ECO:0000313|EMBL:SON48390.1, ECO:0000313|Proteomes:UP000235828};
RN [1] {ECO:0000313|EMBL:SON48390.1, ECO:0000313|Proteomes:UP000235828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vibrio tapetis CECT4600 {ECO:0000313|EMBL:SON48390.1};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-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 topoisomerase GyrA/ParC subunit family.
CC {ECO:0000256|HAMAP-Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
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DR EMBL; LT960611; SON48390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N8Z919; -.
DR KEGG; vta:A0411; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000235828; Chromosome a.
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:UP000235828};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..498
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 845..885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 559..565
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 858..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 885 AA; 97795 MW; 2B25D3DBA370C0A5 CRC64;
MSDLAKEITP VNIEDELRSS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMNVLGNDWN
KSYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SIDGDSAAAM
RYTEVRMSKI AHELLADLDK ETVDYVPNYD GTEQIPAVLP TKIPNLLVNG ASGIAVGMAT
NIPPHNLGEV VDGCLAFINN EDITIDELMD YIPGPDFPTA AMISGRKGIV DAYKTGRGKV
YMRAKANIEA DKNGKETIIV TEIPYQVNKA RLIEKVAELV KDKKVEGISA LRDESDKDGM
RIVIECKRDA VGEVVLNNLY SQTQLQTTFG VNMVALDNGQ PKLFNLKEML KCFVDHRREV
VTRRTIFELK KARDRAHILE ALALALANID EIIALIKNAA TPAEAKEGLV ARGWDLGNVA
SMLERAGTDA ARPDWLEDQF GIRDGQYFLT ETQAQAILEL RLHRLTGLEH EKILDEYKAL
LEEIAELMHI LASTERLMEV IREELEAVRD GFADARRTEI TAAMHDIDME DLITQEDVVV
TLSREGYVKY QILSDYEAQR RGGKGKSATK MKEEDYIERL LVANTHDNIL CFSTRGKTYR
LKVYQLPQAS RTARGKPIVN ILPLEENERI TAILPVSEFS SDKYIFMATG DGTVKKTSLD
QFANVRANGL IAVNLRDDDS LIGVDITNGE NDIMLFSKSG KVVRFAEDKV RAMGRTASGV
RGMKLPEDDQ VVSLIVPANE GDILTVTNNG YGKRTTLAEY PTKGRATQGV VSIKVSDRNG
PVVGAVQVED GDEFMMITDA GTLVRTRVSE VSQVGRNTLG VTLIRTAEDE SVVALQRIDE
IEEAELAEGE ELQEGEEPSS EQPSAESSES TDSTDAPKAD DANEE
//