GYRA_MICLC
ID GYRA_MICLC Reviewed; 898 AA.
AC C5C7X9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
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, ECO:0000269|PubMed:153201, ECO:0000269|PubMed:276855};
GN Name=gyrA {ECO:0000255|HAMAP-Rule:MF_01897}; OrderedLocusNames=Mlut_00060;
OS Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 /
OS NCIMB 9278 / NCTC 2665 / VKM Ac-2230) (Micrococcus lysodeikticus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX NCBI_TaxID=465515;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC
RC 2665 / VKM Ac-2230;
RX PubMed=19948807; DOI=10.1128/jb.01254-09;
RA Young M., Artsatbanov V., Beller H.R., Chandra G., Chater K.F., Dover L.G.,
RA Goh E.B., Kahan T., Kaprelyants A.S., Kyrpides N., Lapidus A., Lowry S.R.,
RA Lykidis A., Mahillon J., Markowitz V., Mavromatis K., Mukamolova G.V.,
RA Oren A., Rokem J.S., Smith M.C., Young D.I., Greenblatt C.L.;
RT "Genome sequence of the Fleming strain of Micrococcus luteus, a simple
RT free-living actinobacterium.";
RL J. Bacteriol. 192:841-860(2010).
RN [2]
RP FUNCTION IN NEGATIVE SUPERCOILING, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP SUBUNIT, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=276855; DOI=10.1073/pnas.75.5.2098;
RA Liu L.F., Wang J.C.;
RT "Micrococcus luteus DNA gyrase: active components and a model for its
RT supercoiling of DNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:2098-2102(1978).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND
RP DNA-BINDING.
RX PubMed=153201; DOI=10.1016/0092-8674(78)90281-7;
RA Liu L.F., Wang J.C.;
RT "DNA-DNA gyrase complex: the wrapping of the DNA duplex outside the
RT enzyme.";
RL Cell 15:979-984(1978).
CC -!- FUNCTION: A type II topoisomerase that negatively supercoils DNA in an
CC ATP-dependent manner (PubMed:276855). About 140 bp of DNA wraps around
CC gyrase in the presence or absence of ATP, when ATP is added negative
CC supercoils are made (PubMed:153201). {ECO:0000269|PubMed:153201,
CC ECO:0000269|PubMed:276855}.
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-Rule:MF_01897,
CC ECO:0000269|PubMed:153201, ECO:0000269|PubMed:276855};
CC -!- ACTIVITY REGULATION: Supercoiling activity inhibited by novobiocin and
CC coumermycin, DNA wrapping around gyrase is not inhibited
CC (PubMed:276855, PubMed:153201). {ECO:0000269|PubMed:153201,
CC ECO:0000269|PubMed:276855}.
CC -!- SUBUNIT: Heterotetramer, composed of two GyrA and two GyrB chains
CC (PubMed:276855, PubMed:153201). In the heterotetramer, GyrA contains
CC the active site tyrosine that forms a transient covalent intermediate
CC with the DNA, while GyrB bind cofactors and catalyzes ATP hydrolysis.
CC {ECO:0000255|HAMAP-Rule:MF_01897, ECO:0000269|PubMed:276855}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01897,
CC ECO:0000269|PubMed:276855}.
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; CP001628; ACS29581.1; -; Genomic_DNA.
DR RefSeq; WP_010079769.1; NZ_WBMF01000017.1.
DR AlphaFoldDB; C5C7X9; -.
DR SMR; C5C7X9; -.
DR STRING; 465515.Mlut_00060; -.
DR PRIDE; C5C7X9; -.
DR EnsemblBacteria; ACS29581; ACS29581; Mlut_00060.
DR KEGG; mlu:Mlut_00060; -.
DR PATRIC; fig|465515.4.peg.6; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_11; -.
DR OMA; THHWLLF; -.
DR OrthoDB; 217468at2; -.
DR Proteomes; UP000000738; 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; IDA:UniProtKB.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IDA:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW Reference proteome; Topoisomerase.
FT CHAIN 1..898
FT /note="DNA gyrase subunit A"
FT /id="PRO_0000435477"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 852..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 566..572
FT /note="GyrA-box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
FT ACT_SITE 158
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01897"
SQ SEQUENCE 898 AA; 99097 MW; 380C59F1AA822A15 CRC64;
MSDETTPQTP DEPVEGAPIP GTPQTGLDIE VEHYVLPEGA ADKVEPVDLE SEMKRSYLDY
AMAVIVGRAL PDVRDGLKPV HRRVLYAMYD GGYRPDRAFN KSARVVGDVM GNYHPHGDTA
IYDALVRLIQ DWVQRYPLAL GQGNFGSPGN DGAAAQRYTE TKMAPLAMEM VRDIDEDTVD
MQDNYDGKQQ EPVVLPARYP NLLVNGSSGI AVGMATNIPP HNMREVAAGV QWYLEHPEAT
REELLEALLA RVHGPDFPTG AQILGRKGIE EVYRTGRGPI TMRAVVNVEE IQGRTCLVVT
ELPYMTNPDN LAAKIAEMVR DGKISGIADM RDETSGRTGQ RLVIVLKRDA VAKVVLNNLY
KHTELQSNFS ANMLALVDGV PRTLSLDGFV HHWVKHQIDV IVRRTAFRKR KAEERAHILR
GLLKALDMLD EVIATIRRSA SADVAREALK ELLDIDDVQA QAILQMQLRQ LAALESQKIQ
DEYDDLMAKI AEYNRILESP QRQREVISEE LAEIVAKHGD DRRTEIMAGF DGDMSIEDLI
PEEEMVVSIT RGGYVKRTRI DQYRSQARGG KGVRGATLRG DDVVEHFLTV STHHWLLFFT
NFGRVYRIKT YELLEAGRDA KGQHVANLLA FQPDERIAQI QPLVDYGRAP YLVLATRGGL
VKKTPLLDYD TNRTAGLIAI KLREGDELVS ARVVSPDDDL ILISHKGQSL RFTATDEALR
PMGRATSGVT GMKFRDDDSL LTMDVVEEDG YVFTVTDGGF AKRTHVDEYR LQNRGGLGIK
VAKLVDDRGE LAGGLVVRED QEVLVVMASG KVVRSAVAGV PAKGRDTMGV IFAKPDKRDR
IVAVTLNNEQ EMEAKADAEA EAGPDVPLDA DIDPTDPVAA PEDALTQDAG EGADGGEQ
