ID A0A086D3I1_9GAMM Unreviewed; 917 AA.
AC A0A086D3I1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, 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=GY26_10560 {ECO:0000313|EMBL:KFF48995.1};
OS Gammaproteobacteria bacterium MFB021.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=1492922 {ECO:0000313|EMBL:KFF48995.1, ECO:0000313|Proteomes:UP000028732};
RN [1] {ECO:0000313|EMBL:KFF48995.1, ECO:0000313|Proteomes:UP000028732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFB021 {ECO:0000313|EMBL:KFF48995.1,
RC ECO:0000313|Proteomes:UP000028732};
RA Joseph T.C., Baby A., Varghese A.M., Reghunathan D., Murugadas V.,
RA Lalitha K.V.;
RT "Draft Genome sequence of a halophilic and highly halotolerant unknown
RT Gammaproteobacteria strain MFB021.";
RL Submitted (JUN-2014) 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: 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:KFF48995.1}.
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DR EMBL; JNVT01000074; KFF48995.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086D3I1; -.
DR STRING; 1492922.GY26_10560; -.
DR eggNOG; COG0188; Bacteria.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000028732; 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; 7.
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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..501
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 879..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 562..568
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 884..899
FT /note="Acidic 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 917 AA; 101547 MW; 6F2B35BD51E3BE77 CRC64;
MGDIAREILP VNIEDELKQS YLDYAMSVII GRALPDVRDG LKPVHRRVLY AMHELGNDWN
KPYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQHFSMRH VLIDGQGNFG SIDGDNAAAM
RYTEVRMARL SHELLADLEK DTVDWVDNYD GTERIPEVLP TKVPNLLING ASGIAVGMAT
NIPPHNMVEV ISGCLALIQD YTLTVDDLME YIPGPDFPTA GIINGRAGIL EAYRTGRGRI
YVRARHTVEF DKKSGRDQIV ITELPYQVNK ARLIEKIAEL VKEKRVEGIA ELRDESDKDG
LRVVIEIKRG ESGDVVVNNL FAHTQLETVF GINIVALHDG QPKTLNLKEL LEAFIRHRRE
VVTRRTLFEL KKARERGHIL EGLAVAISNI DEVIELIKAS PNAAEAKEKL IARDWQPGQV
TGMLERAGAT SCKPEDLDEG YGLTDDRALY RLSPAQAQAI LELRLHRLTG LETEKLLDEY
LSILERIAEL NHILASPDRL LEVIREELEG IRDQYGNARL TEIQTSRLDL TMEDLIAEED
MVVTLSRGGY AKTQPISDYQ AQKRGGRGKS ATSMKDEDVI EHLVVASTHD TMLLFSNRGK
VYWLKTYEMP NASRGSRGKP LVNLLPLDDG ESINAILPVR DYNPESYIFF ATASGTVKRT
SLDQFSRPRS VGLIAIGLGE GDRLIGAAIT SGNDHVMLLS SDGKAIRFEE RYEKIVSEDG
SEKTKGVPPM GRNARGVRGM RLKDGAEVIS LIIPQSQTID ADADNELDGD TATSADGSEE
QIYILTASEH GYGKRTRLEE FPIRGRGGQG VIAMQTTERN GALVAAMQVR DSDEMMLITD
RGTLVRTRVG EVSITSRNTQ GVTLIRTSEG EHLVKTVRVD EPQDEALDEL ETSDESEAGD
AEVPPEKGET PPADDDA
//