(data stored in ACNUC1104 zone)

SWISSPROT: GYRA_NOCSJ

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
//

If you have problems or comments...

PBIL Back to PBIL home page