ID A0A0X8X2Y0_9SPHI Unreviewed; 851 AA.
AC A0A0X8X2Y0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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_2 {ECO:0000313|EMBL:BAU54754.1};
GN Synonyms=gyrA {ECO:0000256|HAMAP-Rule:MF_01897};
GN ORFNames=FHS11_002348 {ECO:0000313|EMBL:MBB3055929.1}, MgSA37_02932
GN {ECO:0000313|EMBL:BAU54754.1};
OS Mucilaginibacter gotjawali.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1550579 {ECO:0000313|EMBL:BAU54754.1, ECO:0000313|Proteomes:UP000218263};
RN [1] {ECO:0000313|EMBL:BAU54754.1, ECO:0000313|Proteomes:UP000218263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA3-7 {ECO:0000313|EMBL:BAU54754.1,
RC ECO:0000313|Proteomes:UP000218263};
RA Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT "Genome sequence of Mucilaginibacter gotjawali.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3055929.1, ECO:0000313|Proteomes:UP000539265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8628 {ECO:0000313|EMBL:MBB3055929.1,
RC ECO:0000313|Proteomes:UP000539265};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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}.
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DR EMBL; AP017313; BAU54754.1; -; Genomic_DNA.
DR EMBL; JACHWX010000005; MBB3055929.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X8X2Y0; -.
DR KEGG; mgot:MgSA37_02932; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000218263; Chromosome.
DR Proteomes; UP000539265; 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:UP000218263};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 19..472
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 816..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 533..539
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 832..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 130
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 851 AA; 95497 MW; 2DA6CF19F8D0582D CRC64;
MAEETGNGNT PPEDRIISIN IDEEMRSAYI DYSMSVIVSR ALPDVRDGLK PVHRRVLYGM
LDLGLNNNKP YKKSARIVGE VLGKYHPHGD TSVYDAMVRM AQDWSLRYPF VEGQGNYGSI
DGDQPAAMRY TEARLEKIAE EMLADINKDT IDFQLNFDDS LEEPTVLPAK FPNLLVNGAS
GIAVGMATNM APHNLTEVVN ATLALIDNRD IDIAELMTHI KGPDFPTGAI IYGYEGARQA
FETGRGRIVI RSRAEIETYN NDRERIIVSE VPYQVNKALM IERTAELVNE KKIEGISAIR
DESNREGIRV VYEIKRDANA AIVLNNLYKY TALQTSFSIN NIALVHGRPM LLNLKDLIHH
FVEHRHEVVI RRTKFELSEA QKRAHILEGL LIALDHLDEV IKLIRGSNTP EDAREGLMAQ
FALSDIQARA ILDMTLRRLT GLERDKIKDE YEGLMKLIDY LNSVLADEGL RMQIIKDELI
EIRDKYGDER KTEMVHSSAE MNTEDFIEDE DVVITISREG YIKRTPLTEY RRQGRGGKGS
LGSNSRDADF IEHLLIASNH NYMLFFTESG QCFWLRVFEI PEGSRTSKGR AIQNIINIPK
EENIKAYIKL LSLKDKEYLE NNFIIMCTKK GTIKKTSLEA YSRPRANGIN AININEGDSL
LEASLTSGSS EIVMALKSGR AIRFNESTVR PMGRTATGVR GISLEDENDE VVGMISIDDP
ETTVLVVSEK GYGKRTDIDD YRVTNRGGKG VKTLNITDKT GKLVAIKGVT DKEDLMIINK
SGIIIRIAVS ELRTMGRATQ GVRLITLKEN DEIASVAKIE REEEEEENGT ENNSENNSTE
PAADDAGETQ E
//
