ID W1NBT7_9GAMM Unreviewed; 921 AA.
AC W1NBT7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
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=BJB45_15440 {ECO:0000313|EMBL:ERL52671.1};
OS Halomonas huangheensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1178482 {ECO:0000313|EMBL:ERL52671.1, ECO:0000313|Proteomes:UP000019113};
RN [1] {ECO:0000313|EMBL:ERL52671.1, ECO:0000313|Proteomes:UP000019113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJGMM-B45 {ECO:0000313|EMBL:ERL52671.1,
RC ECO:0000313|Proteomes:UP000019113};
RA Miao C., Wan Y., Jin W.;
RT "draft genome of Halomonas huanghegensis, strain BJGMM-B45T.";
RL Submitted (AUG-2013) 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:ERL52671.1}.
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DR EMBL; AVBC01000014; ERL52671.1; -; Genomic_DNA.
DR RefSeq; WP_021817295.1; NZ_CP013106.1.
DR AlphaFoldDB; W1NBT7; -.
DR STRING; 1178482.AR456_11220; -.
DR KEGG; hhu:AR456_11220; -.
DR PATRIC; fig|1178482.3.peg.344; -.
DR eggNOG; COG0188; Bacteria.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000019113; 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:UP000019113};
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 876..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 487..521
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 562..568
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 894..908
FT /note="Polar 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 921 AA; 101418 MW; B31DE0C12DA64CE3 CRC64;
MGDIAREILP VNIEDELKQS YLDYAMSVII GRALPDVRDG LKPVHRRVLF AMHELSNDWN
KPYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQNFSMRH VLVDGQGNFG SIDGDNAAAM
RYTEVRMARL AHELLADLEK DTVDWVDNYD GTERIPDVLP TRVPNLLING SSGIAVGMAT
NIPPHNMVEI INGCLALIDD YTLTVDDLME YIPGPDFPTG GIINGRAGIL DAYRTGRGRI
YVRACHTIEH DDKSGRDHII VTELPYQVNK ARLIEKIAEL VKDKKIDGIA ELRDESDKDG
LRVVIEVKRG ESGDVVVNNL FAQTQLQNVF GINMVALEDG EPKTMNLKQV LEAFIRHRRE
VVTRRTLFEL RKARERGHIL EGLAVAISNI DEVIELIKAS PNAAEAREKL LARGWQPGQV
TDMLERAGAT SCKPEDLEEG YGLLEGSSEY RLSPAQAQAI LELRLHRLTG LETEKLLDEY
LSILKSIAEL MAILASSERL LEVIREELEA VRDQYGDERR TEIQASRLDL SIEDLIAEED
MVVTVSRSGY AKTQPLSDYQ AQRRGGRGKS ATSMKDEDVI EHLLVASTHD TVLLFSNRGK
VYWLKVYEMP AASRGSRGKP LVNMLPLEEG ESINAILPVN EYDPNCYIFF ATASGTVKRT
SLEQFSRPRS VGLIAIDLEE GDRLIGAAIT SGSDHAMLLS SNGKAIRFEE TQVRAMGRTA
RGVRGMRLLG GAEVISLIIP QSREIDADAD AGEEEAVAVE QGTSSDDQIY ILTASENGYG
KRTRLEEFPL RGRGGQGVIA IQTSERNGSM VAAMQVYSSD EMMLITDRGT LVRTRVGEVS
ITSRNTQGVM LIRLGEAESL VKTVRIEELD EEDVVAEVDG ETVDGGDIEN GAGNTDAGDN
SSGESQADDD AAEGSGNDNE E
//
