ID A0A0R0C9P5_9GAMM Unreviewed; 902 AA.
AC A0A0R0C9P5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=ABB26_14440 {ECO:0000313|EMBL:KRG62878.1};
OS Stenotrophomonas humi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG62878.1, ECO:0000313|Proteomes:UP000050864};
RN [1] {ECO:0000313|EMBL:KRG62878.1, ECO:0000313|Proteomes:UP000050864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG62878.1,
RC ECO:0000313|Proteomes:UP000050864};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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:KRG62878.1}.
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DR EMBL; LDJI01000027; KRG62878.1; -; Genomic_DNA.
DR RefSeq; WP_057635364.1; NZ_LDJI01000027.1.
DR AlphaFoldDB; A0A0R0C9P5; -.
DR STRING; 405444.ABB26_14440; -.
DR PATRIC; fig|405444.3.peg.1994; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000050864; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..498
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 873..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 559..565
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 902 AA; 99110 MW; 46F43251EEF04E7F CRC64;
MAENAKEIIQ VNLEDEMRKS YLDYAMSVIV GRALPDARDG LKPVHRRVLF AMSELGAHSN
KPYYKSARIV GDVIGKYHPH GDQSVYDTLV RLAQPFSLRY MLVDGQGNFG SVDGDSAAAM
RYTEARMSRL AHELMADLDK ETVDFQPNYD EKEMEPTVMP TRFPNLLVNG SAGIAVGMAT
NIPPHNLTES INACIALIDD PSIEVDALME FIPGPDFPTA GIINGTAGII AGYRTGRGRV
RIRARADIEV ADNGRESIIV TEIPYQVNKA RLIEKIAELV KEKKLEGISE LRDESDKDGM
RIYIEIKRGE SAEVVLNNLY QQTQMESVFG INMVALIDGR PKLMNLKQML EAFLRHRREV
VTRRTIFELR KARARAHVLE GLTVALANID EMIELIKTSA NPAEAKERML TKVWEPGLVG
ALLAASGAEA SRPEDLPKNI GLVNGNYQLS DVQATQILEM RLHRLTGLEQ DRLTEEYKVL
LEVIAGLIRI LENPEVLLQV IREELESVRS EFGDARRTEI RHSEEDLDIL DLIAPEDVVV
TLSRAGYVKR QPASAYRAQR RGGRGRSAAA TKDEDSIEQL WLVNTHDTLL TFTSSGKVFW
LPVHQLPEAG SNARGRPIIN WIALENGERV QAVLPVREYD DSHFVFFATR NGTVKKTPLS
EFAFRLARGK IAINLDEGDA LVGVGLTDGD RDVLLFASNG KTVRFAEDKV RSMGRTATGV
RGIKMVKGEE VVSLIVAESA GGVEDESEDE GNVVEEAVID GGEIADIGAD DAGAQYILTA
TENGYGKRTP LADYPRKGRG TQGVIGIQTS ERNGKLVSAV LVSNDDEVML ISDGGTLVRT
RGSEISRVGR NTQGVTLIRL SKGEKLQAVE RLDASLDDGD DTDDEAGVVV QDAEQAPAAP
EA
//
