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 03-AUG-2022, entry version 100.
DE RecName: Full=DNA gyrase subunit A {ECO:0000255|HAMAP-Rule:MF_01897};
DE EC=5.6.2.2 {ECO:0000255|HAMAP-Rule:MF_01897};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; 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., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA 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 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:0000255|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:0000255|HAMAP-
CC 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:0000255|HAMAP-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 topoisomerases;
CC in organisms with a single type II topoisomerase this enzyme also has
CC to decatenate newly replicated chromosomes. {ECO:0000255|HAMAP-
CC Rule:MF_01897}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_01897}.
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DR EMBL; CP000509; ABL79557.1; -; Genomic_DNA.
DR RefSeq; WP_011753508.1; NC_008699.1.
DR AlphaFoldDB; A1SCM2; -.
DR SMR; A1SCM2; -.
DR STRING; 196162.Noca_0007; -.
DR PRIDE; A1SCM2; -.
DR EnsemblBacteria; ABL79557; ABL79557; Noca_0007.
DR KEGG; nca:Noca_0007; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_11; -.
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: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; 1.10.268.10; -; 1.
DR Gene3D; 2.120.10.90; -; 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; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
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;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..922
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000409830"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 861..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 545..551
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT COMPBIAS 865..889
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 137
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="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
