(data stored in SCRATCH3701 zone)

SWISSPROT: A3CVD7_METMJ

ID   A3CVD7_METMJ            Unreviewed;       811 AA.
AC   A3CVD7;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   11-DEC-2019, entry version 88.
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=Memar_1408 {ECO:0000313|EMBL:ABN57337.1};
OS   Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=368407 {ECO:0000313|EMBL:ABN57337.1, ECO:0000313|Proteomes:UP000002146};
RN   [1] {ECO:0000313|EMBL:ABN57337.1, ECO:0000313|Proteomes:UP000002146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35101 / DSM 1498 / JR1
RC   {ECO:0000313|Proteomes:UP000002146};
RX   PubMed=21304656; DOI=10.4056/sigs.32535;
RA   Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA   Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT   type strain JR1.";
RL   Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN57337.1; -; Genomic_DNA.
DR   RefSeq; WP_011844248.1; NC_009051.1.
DR   STRING; 368407.Memar_1408; -.
DR   EnsemblBacteria; ABN57337; ABN57337; Memar_1408.
DR   GeneID; 4846971; -.
DR   KEGG; mem:Memar_1408; -.
DR   eggNOG; arCOG04367; Archaea.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 1547at2157; -.
DR   BioCyc; MMAR368407:G1G85-1407-MONOMER; -.
DR   Proteomes; UP000002146; 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; A3CVD7.
DR   SWISS-2DPAGE; A3CVD7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897};
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:ABN57337.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897}.
FT   DOMAIN          11..463
FT                   /note="TOP4c"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   MOTIF           524..530
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        122
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   811 AA;  90145 MW;  4D87267FFB2C5B7D CRC64;
     MTSEGEGVVP INIEEEMKSC YIDYAMSVII GRAIPDARDG LKPVHRRTLY AMWEMGNTSD
     KPYKKSARIV GDVMGKYHPH GDSAIYDTLV KMAQPFSYRC MLVDGQGNFG SIDGDSAAAM
     RYTEARLTKI SEELLTDIDK KTVDFVPNFD ESLQEPSVLP ARIPNLLVNG SSGIAVGMAT
     NMPPHNLREV CEATCRVIDD AGTSTEELMQ VMPGPDFPTG GIMMGTAGIR DAYLTGRGKC
     VVRGVAEIEE EGRTPQIIIT EIPFQVNKAR LIEHIASLVR DKRIEGIGDI RDESDRDGMR
     IVVELKRGAA PQVILNFLYK HTALESSFGI INLAIVDRQP RTLNLKEIIH EFLKHRVDVV
     RRRTEFDLTK NEERMHILRG LLVALDNIDA VIATIRGSGT TDEAQKALVA KFALDEVQAD
     AILKMQLRRL AALEHQKILD ERDAIAAEIE RLSAILASEA SILAEIKKEL VDIGARFGDE
     RRTRIAQAAE AFDREDLIED KPVLVSLTSS NYVKRIDLDT YRNQRRGGHG VIGMATKDND
     GVEKVFVANM HDNLLCFTDR GRMYWLKIYD LPEGQRTGKG KALVNLLNLD GEERVTTVIP
     VREYRPDHHL FFATRNGTVA KMALDEFSRP RQTGINAINL RDGDALVDVK ATDGNQELIL
     TTKFGQSLRF HEEAVRPVHR NAMGVRGIKL RHGDALQAIA IVEDDHLLTI TEQGYGKRTE
     FDEYRGHGRG TLGVRNIVVD ARAGNVVGSM AVSDDDEIIV MSASGIVIRT KVSEISIQKR
     GTRGVRVMKL DDGDRVIGFT ILDSEEPEEE A
//

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