ID A0A2G4EYP0_9CYAN Unreviewed; 904 AA.
AC A0A2G4EYP0;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-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=CP500_015060 {ECO:0000313|EMBL:PHX54639.1};
OS Tychonema bourrellyi FEM_GT703.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Tychonema.
OX NCBI_TaxID=2040638 {ECO:0000313|EMBL:PHX54639.1, ECO:0000313|Proteomes:UP000226442};
RN [1] {ECO:0000313|EMBL:PHX54639.1, ECO:0000313|Proteomes:UP000226442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FEM_GT703 {ECO:0000313|EMBL:PHX54639.1,
RC ECO:0000313|Proteomes:UP000226442};
RA Banno H., Chua N.-H.;
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PHX54639.1, ECO:0000313|Proteomes:UP000226442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FEM_GT703 {ECO:0000313|EMBL:PHX54639.1,
RC ECO:0000313|Proteomes:UP000226442};
RA Tett A., Armanini F., Asnicar F., Boscaini A., Pasolli E., Zolfo M.,
RA Donati C., Salmaso N., Segata N.;
RT "Draft genome sequence of the planktic cyanobacteria Tychonema bourrellyi
RT isolated from alpine lentic freshwater.";
RL Submitted (NOV-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-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:PHX54639.1}.
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DR EMBL; NXIB02000087; PHX54639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G4EYP0; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000226442; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000226442};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..469
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 429..475
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 746..778
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 904 AA; 100436 MW; 1A6994D1B270FBA3 CRC64;
MSTSESRIIP TDLGNEMSRS YLEYAMSVIV GRALPDARDG LKPVHRRILY AMNELGLTPD
RPFRKCARVV GEVLGKYHPH GDTAVYDALV RMAQDFSMRE RLINGHGNFG SVDNDPAAAM
RYTECRLTSL TYDAMLRDID CETVDFGDNF DGSQQEPLVL PARIPQILLN GSSGIAVGMA
TNIPPHNLGE VIDGFVALIH NPEITDLELM QYIPGPDFPT GGQILGKATI REAYTTGRGS
ITMRGVASIE TIEHVGRPDK EAIIITELPY QTNKAALIEK IAELVNDKRL EGISDLRDES
DRNGMRIVIE LKRDAYPRVV LNNLYKQTPL QSNFGANMLA LVNGEPQLLS LSQFLNVFLD
FRIETITRRT QYELRKAEER DHLLQGLLIA LENLDGIIQL IRRAPDSAAA KQELIDNYGL
SDQQSDAILQ MQLRRLTALE AQKIQQEHEE LRTKIADLED ILARRERILE IAEVEALEIK
TKIATPRRTV IEHAEGEIDE RDLIANEQAI ILITEQGYIK RMPVSTFEAQ SRATRGKAGT
KMKEDDGVEH FLSCCDHDTV LFFSNRGVVY SVKAYQIPVS SRTARGMPVL QMLPIPMEEK
ITSMVSVTEF STEEYLVMLT RSGYIKKTAL SAFGNIRTNG LIAISLEEGD QLRWVRRAKV
GDSIIIGTSQ GMAIHFRTNH EQLRPTGRAT RGVKSMKLRS GDELISMDIL PSSIVAEIAE
LETGELELDG ANIALLETGD SELESADIAE LETGELELEE EELELEAEEI EGEDAEEITT
ANSEVPSVLV ITTNGYGKRV PVSQFRLQRR AGKGLTATKF KSKKAKDRVA ALRIVNDSDE
LMIITNRGII IRQAVSAIST QSRTATGVRV QRLDEDDSIV AVALVPPSGE ESIEDAESEE
VTEE
//
