(data stored in SCRATCH3701 zone)

SWISSPROT: D5EB23_METMS

ID   D5EB23_METMS            Unreviewed;       824 AA.
AC   D5EB23;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 67.
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   OrderedLocusNames=Mmah_0851 {ECO:0000313|EMBL:ADE36374.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE36374.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE36374.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) 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|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: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 topoisomerase GyrA/ParC subunit family.
CC       {ECO:0000256|HAMAP-Rule:MF_01897}.
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DR   EMBL; CP001994; ADE36374.1; -; Genomic_DNA.
DR   RefSeq; WP_013037317.1; NC_014002.1.
DR   EnsemblBacteria; ADE36374; ADE36374; Mmah_0851.
DR   GeneID; 8983015; -.
DR   KEGG; mmh:Mmah_0851; -.
DR   eggNOG; arCOG04367; Archaea.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 1547at2157; -.
DR   BioCyc; MMAH547558:G1GHT-869-MONOMER; -.
DR   Proteomes; UP000001059; 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 (double strand cut, 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; 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; 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; D5EB23.
DR   SWISS-2DPAGE; D5EB23.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897, ECO:0000313|EMBL:ADE36374.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897}.
FT   DOMAIN          27..480
FT                   /note="TOP4c"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          466..493
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           541..547
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        138
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   824 AA;  92330 MW;  02C9B22C9914B8D8 CRC64;
     MADYDDINPL DEKIEQHDGE GGRVVPVLIQ DEMKRSYIDY SMSVIVGRAL PDARDGLKPV
     HRRILHSMNE AGITHDKAYK KSARVVGDVL GKFHPHGDTA VYDSLVRMVQ DFSLRYPLID
     GQGNFGSVDG DSAAAMRYTE VRMDKITTEM LEDIKKGTVD FKPNYDGSLE EPEVLPSKLP
     NLLLNGSTGI AVGMATNMAP HNLGEVVDAT VKLIDDPETE LAELRKIVKG PDFPTGGIIM
     GTSGIKSAYE TGRSPIYLRA VTEIEEMKND KYRIVVYELP YQVNKARLVE SIANLVRDKK
     IEGISDLRDE SGREGMRVVI ELKKAANPKV LLNQLYKQTQ LETTFGIINL ALVDGVPRVL
     NLRELIQIYL KHRIDVISRR TVFDLRKAEE RAHILQGLKV ALDNIDEVIK LIRGSSTTEE
     AREGLISNFD LDEIQAKAIL DMKLQRLTGL ERQKIDEEYN GLIDTIADLK DILANDERKY
     AIIRDEVLEL KDKYGDERRT LIQSSREELA DEDLIPEEEV VVTSTQSGYI KNIPLQTYNM
     QHRGGRGVRG METKEDDTVG SIFVASTHDY ILFFTNRGKV YWQKVYDIPR GSRQSRGKAI
     VNLLELAEGE SVNAMIPVHD FENDRYLFMG TRDGTVKRCS LSDFSNPRKA GIIAISLKEG
     DELVNVLQTD GNQDIMLASR HGKALRISEE DVRVMGRTAR GVRGMKLAGP DVIVSLDVVD
     SDGTLLTVTE NGFGKRTPFD EYRTLRRGGQ GVITIFTDMR NGPVVTVKTV EDDDEIILTS
     SAGIVMRIPV TDIRVQGRNT KGVKIMNIRE KDKLVSLARI KKEE
//

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