ID U5C452_9BACT Unreviewed; 851 AA.
AC U5C452;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=P872_04965 {ECO:0000313|EMBL:ERM82967.1};
OS Rhodonellum psychrophilum GCM71 = DSM 17998.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Rhodonellum.
OX NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM82967.1, ECO:0000313|Proteomes:UP000016843};
RN [1] {ECO:0000313|EMBL:ERM82967.1, ECO:0000313|Proteomes:UP000016843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GCM71 {ECO:0000313|EMBL:ERM82967.1,
RC ECO:0000313|Proteomes:UP000016843};
RX PubMed=24309741;
RA Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.;
RT "Draft Genome Sequence of the Psychrophilic and Alkaliphilic Rhodonellum
RT psychrophilum Strain GCM71T.";
RL Genome Announc. 1:e01014-13(2013).
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:ERM82967.1}.
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DR EMBL; AWXR01000019; ERM82967.1; -; Genomic_DNA.
DR RefSeq; WP_019598819.1; NZ_KB906682.1.
DR AlphaFoldDB; U5C452; -.
DR PATRIC; fig|1123057.7.peg.2101; -.
DR eggNOG; COG0188; Bacteria.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000016843; 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:UP000016843};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 12..465
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 823..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 451..485
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 526..532
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 823..845
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 851 AA; 95783 MW; 0EF25572EB02B7AB CRC64;
MAQGENENII PINIEDEMRG AYIDYSMSVI VSRALPDVRD GLKPVHRRIL FGMQELGVLH
NKSHKKSARI VGEVLGKYHP HGDSAVYETM VRMAQPWSLR YPLVDGQGNF GSVDGDNPAA
MRYTEARLKR IAEELLIDIN KETVDFQLNF DDSLKEPIVL PAKIPALLLN GASGIAVGMA
TNMAPHNLGE IVDGIHAFID NRDITVEELM QFIIAPDFPT GGTIYGYNGV KAAFETGRGR
VIIRGKSNIE VKENGREMII ITEIPYLVNK ANMIEKTAQL ITEKKIDGIS AIRDESDRTG
MRIVYELKKD AMPSVILNNL YRQTQLQTSF SVNNVALVKG RPYTLNLKDM IFHYVNHRHE
VVIRRTEYEL REAQKRAHIL EGYLIALDHL DEVISLIRSS KDPETARNGL MERFKLSEIQ
ARAILDMRLQ RLTGMERDKI QDEYNEIMSM IEEYNAILAS EEKRMQIIKD ELTEIRTRYA
DARRTEIEHN AEDFNYEDMI PNEEVVITVS HEGYVKRTAL TEYKTQGRGG VGSKGATTKL
DDWTEYLFTA STHNYLLIFT DLGKLFWLKT YAIPEGAKAS RGRPIQNLIQ IESNDKIRSI
IQVGNLNDAD YINNNFLVMV TKQGIIKKTT LEQYSRPRSN GIIALNIRED DQLIQVEMTN
GDSHILIAAK SGRAIHFHES KVRPMGRTAT GVKAIKLSDV NDYVIGMVCA DSHETSLLVV
SEKGYGKRSP LGEYRITNRG GKGVKAMNVT EKTGSLVAIK QVMDSDDLMI INKSGITIRT
PVSELRIMGR ATQGVRLIKL GENDEISSVE KIKNEESIVL EIEATDDLDL GTDNSIPDED
SENTNTEEPN P
//
