ID V9G8F3_9BACL Unreviewed; 839 AA.
AC V9G8F3;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=JCM10914_2287 {ECO:0000313|EMBL:GAE06143.1};
OS Paenibacillus sp. JCM 10914.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236974 {ECO:0000313|EMBL:GAE06143.1, ECO:0000313|Proteomes:UP000018028};
RN [1] {ECO:0000313|EMBL:GAE06143.1, ECO:0000313|Proteomes:UP000018028}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10914 {ECO:0000313|EMBL:GAE06143.1,
RC ECO:0000313|Proteomes:UP000018028};
RA Ohkuma M., Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida T.,
RA Hattori M.;
RT "Draft Genome Sequence of the Alkaliphilic and Xylanolytic Paenibacillus
RT sp. Strain JCM 10914, Isolated from the Gut of a Soil-Feeding Termite.";
RL Genome Announc. 2:e01144-13(2014).
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:GAE06143.1}.
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DR EMBL; BAUO01000006; GAE06143.1; -; Genomic_DNA.
DR RefSeq; WP_023960139.1; NZ_BAZR01000006.1.
DR AlphaFoldDB; V9G8F3; -.
DR STRING; 1236974.GCA_001315105_02230; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000018028; 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:UP000018028};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 12..464
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 800..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 436..484
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 525..531
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 123
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 839 AA; 94569 MW; 23B209D5CC712446 CRC64;
MAEENFSQIK DRDIGTEMRE SFMDYAMSII VSRALPDVRD GMKPVHRRIL YAMSELGMAP
DKPHKKSARI VGEVIGKYHP HGDSAVYESM VRMAQDFSMR YMLVDGHGNF GSIDGDMAAA
MRYTEARLSK IAMEMLRDIN KETIDFAPNY DGEEQEPVVL PARYPNLLVN GVSGIAVGMA
TNIPPHNLGE VIDGVQAMIR NPDITPMELM EYIQGPDFPT AGYILGREGI RQAYRTGRGS
VTMRAKATIE ENNNKARIVV HEIPYQVNKA RLVEKIAELV REKRIDGITD LRDESDRNGM
RIVIELRRDV NPNVVLNNLY KHTAMQSNFG INMLAIVNNE PKILNLRDVL FHYLEHQVIV
IRRRTEFELR KAEARAHILE GLRIALDHLD EVIALIRASQ TTEAAREGLM GRFGLSQEQA
QAILDMRLQR LTGLEREKIE NEYQELLAKI AELREILANE HLVLQIINDE LQEIKERFSD
ERRTEITVGE DSILDEDLIP REEVIITITH TGYIKRLPAN TYRSQKRGGR GVVGMDTKSE
DFVEHLFVTN SHHYLMFFTD KGKAYRLKAY EIPELSRTAR GTPIINLIQI EQGESINAVI
PVENFDSDNF LFFATHQGVV KKTPLEDYVN IRKGGLIAIN LREDDSLIEV KLTDGQQEII
MGTAQGMSIR FKESDVRSMG RSATGVKGIT LDDHDEVIGM DVVDQELDIL IVTTKGYGKR
TPASDYRSQT RGGKGIKTIN ITEKNGPVVA LKVVKSEEDL MIITSSGTII RTSMEGISTM
GRYAQGVKLI NIREDDSVGT VCRADKSDEP EEIEDEEWVE GSETAGPVDS EDPIDPTEE
//
