ID A0A097R3Y9_HAFAL Unreviewed; 889 AA.
AC A0A097R3Y9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, 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=AT03_14335 {ECO:0000313|EMBL:AIU73447.1};
OS Hafnia alvei FB1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Hafnia.
OX NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU73447.1, ECO:0000313|Proteomes:UP000029986};
RN [1] {ECO:0000313|EMBL:AIU73447.1, ECO:0000313|Proteomes:UP000029986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FB1 {ECO:0000313|EMBL:AIU73447.1,
RC ECO:0000313|Proteomes:UP000029986};
RX PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA Tan J.Y., Yin W.F., Chan K.G.;
RT "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT pathogenesis: a draft genome perspective.";
RL Gut Pathog. 6:29-29(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}.
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DR EMBL; CP009706; AIU73447.1; -; Genomic_DNA.
DR RefSeq; WP_025798035.1; NZ_CP009706.1.
DR AlphaFoldDB; A0A097R3Y9; -.
DR KEGG; hav:AT03_14335; -.
DR PATRIC; fig|1453496.5.peg.2925; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_6; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000029986; Chromosome.
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:UP000029986};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..499
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 841..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 560..566
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 843..889
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 889 AA; 98418 MW; B949E754A877C9B8 CRC64;
MSDLAREITP VNIEEELKNS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF AMNVLGNDWN
KAYKKSARIV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY MLVDGQGNFG SVDGDSAAAM
RYTEIRMSKI AHELLADLEK ETVDFVPNYD GTEQIPAVLP TKVPNLLVNG SSGIAVGMAT
NIPPHNLNEV INGCLAYIDD ENITVEGLMQ HIPGPDFPTA AIINGRRGIE EAYRTGRGKV
YIRAKAEVEA DEKTGRETII VHEIPYQVNK ARLIEKIAEL VKEKRLEGIS ALRDESDKDG
MRIVIEIKRD AVGEVVLNHL YSLTQMQVTF GINMVALHQG QPKLLTLKDC LQAFVRHRRE
VVTRRTIFEL RKARDRAHIL EGLAIALSNI DPIIELIRRA PNPAEAKALL VARGWELGTV
AAMLERAGDN AARPEWLEPE FGIRDGHYYL TEQQAQAILD LRLQKLTGLE HEKLLDEYKD
LLEQIAALIF ILESPDRLME VIREELIAVR DQFGDARRTE ITENTADINI EDLISQEDVV
VTLSHQGYVK YQPLTDYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDTI LCFSSRGRLY
WMKVYQLPEA SRGARGRPII NLLPLEANER ITAILPVREY EEGRHVFMAT ASGTVKKTAL
TDFSRPRSAG IIAVNLNEGD ELIGVDLTDG SNEVMLFSAA GKVVRFPESQ VRSMGRTATG
VRGINLNGED RVVSLIIPRG EGDILTVTEN GYGKRTGVAE YPTKSRATQG VISIKVSERN
GNVVGAVQVD ECDQIMMITD AGTLVRTRVA EVSVVGRNTQ GVTLIRTAED EHVVGLQRVA
EPEEDDEVLD GEENAAVDGD VADVADVADD AESVDDASES DDEEGDENA
//
