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ID GYRA_NOCSJ Reviewed; 922 AA.
AC A1SCM2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 08-MAY-2019, entry version 90.
DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.3 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897};
GN OrderedLocusNames=Noca_0007;
OS Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC Nocardioides.
OX NCBI_TaxID=196162;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA Pitluck S., Thompson L.S., Brettin T., Bruce D., Han C., Tapia R.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Mattes T., Gossett J., Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils
CC closed circular double-stranded (ds) DNA in an ATP-dependent
CC manner to modulate DNA topology and maintain chromosomes in an
CC underwound state. Negative supercoiling favors strand separation,
CC and DNA replication, transcription, recombination and repair, all
CC of which involve strand separation. Also able to catalyze the
CC interconversion of other topological isomers of dsDNA rings,
CC including catenanes and knotted rings. Type II topoisomerases
CC break and join 2 DNA strands simultaneously in an ATP-dependent
CC manner. {ECO:0000255|HAMAP-Rule:MF_01897}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.3; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01897};
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains.
CC In the heterotetramer, GyrA contains the active site tyrosine that
CC forms a transient covalent intermediate with DNA, while GyrB binds
CC cofactors and catalyzes ATP hydrolysis. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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
CC topoisomerases; in organisms with a single type II topoisomerase
CC this enzyme also has to decatenate newly replicated chromosomes.
CC {ECO:0000255|HAMAP-Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
DR EMBL; CP000509; ABL79557.1; -; Genomic_DNA.
DR RefSeq; WP_011753508.1; NC_008699.1.
DR SMR; A1SCM2; -.
DR STRING; 196162.Noca_0007; -.
DR PRIDE; A1SCM2; -.
DR EnsemblBacteria; ABL79557; ABL79557; Noca_0007.
DR KEGG; nca:Noca_0007; -.
DR eggNOG; ENOG4105C24; Bacteria.
DR eggNOG; COG0188; LUCA.
DR HOGENOM; HOG000076278; -.
DR KO; K02469; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000640; 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:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd00187; TOP4c; 1.
DR Gene3D; 1.10.268.10; -; 1.
DR Gene3D; 3.90.199.10; -; 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; IPR002205; Topo_IIA_A/C.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR Pfam; PF03989; DNA_gyraseA_C; 6.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; SSF101904; 1.
DR SUPFAM; SSF56719; SSF56719; 1.
PE 3: Inferred from homology;
DR PRODOM; A1SCM2.
DR SWISS-2DPAGE; A1SCM2.
KW ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW Nucleotide-binding; Reference proteome; Topoisomerase.
FT CHAIN 1 922 DNA gyrase subunit A.
FT /FTId=PRO_0000409830.
FT MOTIF 545 551 GyrA-box. {ECO:0000255|HAMAP-
FT Rule:MF_01897}.
FT ACT_SITE 137 137 O-(5'-phospho-DNA)-tyrosine intermediate.
FT {ECO:0000255|HAMAP-Rule:MF_01897}.
SQ SEQUENCE 922 AA; 100698 MW; CA03D88E3556A0FD CRC64;
MTETPTDGGS TPPSDGGGPG GRIEPVELQT SMQRAYIDYA MAVIVGRALP DVRDGLKPVH
RRVLYAMYDG GYRPDRGFSK CSRVVGDVMG QYHPHGDTAI YDTLVRLAQP WVMRAPLIHG
QGNFGSPGND SAAAMRYTEC RMAPLAMEMV RDINEDTVDF QPNYDGRSQE PVVLPARFPN
LLVNGSAGIA VGMATNIPPH NLREVAEGAR WALEHPDATR EELQDALIER IKGPDFPNGA
LIVGRQGIEQ AYRTGRGSIT QRAVIEVDED AKGRTNLVIT ELPYMVNPDN LALKIAELAD
SGKVQGISDV RDDTSDRTGQ RLVVVLKRDA VARVVLNNLL KHTELQTNFS ANMLALVDGV
PRTLAIDQFI SNWVTHQIDV IRRRTEYRLA EAEKRAHVLR GLVKALDMLD EVIALIRRSP
DVAEAREGLI ALLDIDEVQA TAILDMQLRQ LAALQRQKII DDLAEIEARI ADLKDILANV
ARQRQIVADE LAEIVERYGD DRRSQIIAAD GDLSMEDLIP DEELVVSITR GGYAKRTRAD
QYRTQRRGGK GVRGATLRGD DVVEHFIATT NHHWLLFFTT AGRVYRTKAY NLPEASRDAK
GGHVAGLLSF QPDENIAQVL AIRDYDQAPY LVLATRDGLV KKTRLGDYNS PRQAGVIAIN
FRSEDDELIG AELVNPEDHI LLVSRKGQSV RFQADDSQLR PMGRATGGVT GMKFRDGDSL
LSMSVIRAAQ VEAEEAAEAS GESVEEMAET RGQWFGLHPQ YVFTITDGGF AKRTQIPEYR
VQSRGGIGIR AMKLANEDRG ELVGAFIVED GDEILSITSG GQVVRSPIDE NFRPTGRSTM
GVKFVTPKKG DSVAVVARSV EANGDDELDE LDESALDEGG AEGGEVDESA DAGTDATIDG
SAASDVARTE GDTEPDPGES DG
//
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