(data stored in SCRATCH3701 zone)

SWISSPROT: E1QXK9_OLSUV

ID   E1QXK9_OLSUV            Unreviewed;       929 AA.
AC   E1QXK9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   11-DEC-2019, entry version 69.
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=Olsu_1774 {ECO:0000313|EMBL:ADK68862.1};
OS   Olsenella uli (strain ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 /
OS   NCIMB 702895 / VPI D76D-27C) (Lactobacillus uli).
OC   Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC   Olsenella.
OX   NCBI_TaxID=633147 {ECO:0000313|EMBL:ADK68862.1, ECO:0000313|Proteomes:UP000000333};
RN   [1] {ECO:0000313|EMBL:ADK68862.1, ECO:0000313|Proteomes:UP000000333}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49627 / DSM 7084 / CIP 109912 / JCM 12494 / NCIMB 702895 /
RC   VPI D76D-27C {ECO:0000313|Proteomes:UP000000333};
RX   PubMed=21304694; DOI=10.4056/sigs.1082860;
RA   Goker M., Held B., Lucas S., Nolan M., Yasawong M., Glavina Del Rio T.,
RA   Tice H., Cheng J.F., Bruce D., Detter J.C., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Sikorski J., Pukall R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Olsenella uli type strain (VPI D76D-27C).";
RL   Stand. Genomic Sci. 3:76-84(2010).
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-Rule:MF_01897,
CC         ECO:0000256|SAAS:SAAS01218217};
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}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|SAAS:SAAS01062860}.
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DR   EMBL; CP002106; ADK68862.1; -; Genomic_DNA.
DR   RefSeq; WP_013252613.1; NZ_JQCO01000002.1.
DR   STRING; 633147.Olsu_1774; -.
DR   EnsemblBacteria; ADK68862; ADK68862; Olsu_1774.
DR   KEGG; ols:Olsu_1774; -.
DR   PATRIC; fig|633147.7.peg.1481; -.
DR   eggNOG; ENOG4105C24; Bacteria.
DR   eggNOG; COG0188; LUCA.
DR   HOGENOM; HOG000076278; -.
DR   KO; K02469; -.
DR   OMA; THHWLLF; -.
DR   OrthoDB; 217468at2; -.
DR   BioCyc; GCF_001437585:G1EOJ-1461-MONOMER; -.
DR   Proteomes; UP000000333; 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; E1QXK9.
DR   SWISS-2DPAGE; E1QXK9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062880}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062879};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01897, ECO:0000256|SAAS:SAAS00972514,
KW   ECO:0000313|EMBL:ADK68862.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS01062871};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000333};
KW   Topoisomerase {ECO:0000256|HAMAP-Rule:MF_01897,
KW   ECO:0000256|SAAS:SAAS00974554}.
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          884..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          511..531
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           600..606
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   COMPBIAS        16..40
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..929
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        197
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   929 AA;  103015 MW;  2D17576CABBE1097 CRC64;
     MADDNSNITP EDGEHAAASL PDDLRELLDR AERDESGTPV YDPEAEDEAG MDDVATDEAD
     DEVEMGSDNR GMGDDVDIHG GRLQLHEFGH EMEQSFIEYS MSVITARALP DVRDGLKPVH
     RRILYAMNEA GIFPNKPHKK SAWTVGEVIG KYHPHGDSAV YDAMVRLAQW FSMRTPLVDG
     HGNFGNIDGD SAAAMRYTES RLARPAMELL RDLNKDTIDW QSNYDESLQE PVVLPARFPN
     LLVNGSQGIA VGMATNIPPH NLKETIAAVC MLIDNPDATV DDLMTVMPGP DFPTGAVIMG
     SEGIRQAYET GRGIITIRAK AHVESTKTGR NKLVFTEFPY GVNKGTLQEK IAQLVNEKRV
     EGISDMRDES NRKGLRLVIE LKQGAIPEVV LNNLYKYSAL QSSFGIIDLA LVNGVPRTLT
     LREMLQHYID HQVDVVTRRT RFDLAKARAR AHILEGLLLA LDHIDEVISI IRSSRTDTQA
     SERLIERFGF TKQQTTAILE MRLRRLTGLE RDKIQEELDG LRRAIEYYED LLADSRKILE
     VIKSEMSEIG EKYGDKRRTT ISDAPVVLDV EDLIAEEDMV VTVTHAGYVK RLPVATYRSQ
     KRGGKGVQGL SLKDNDFVED LFVASTHDYV MFFTNRGKVY RVKVHELPIG SRHARGSALV
     NVLPLGEGEH PTAVITTREF PADEYLMFAT ANGMVKKTAM SDYDKSRRDG IIAINLKRDD
     ELVNVRRVKP GQKVILCSEV GKAILFDESE VRPTGRDTSG VRGITLKDDV KMLGMEITNG
     NGDLLVMTER GYGKRTPVFE YPEHKRGGQG VATIAMTSKK GNLVACRVVG PQHELMIVSE
     EGVVIRVKTA DISKLGRATQ GVKIMNMGEN DKVSAVARMV AHKKKAAKAN PMQRSLDLSA
     AGARDASDED PVDIGDEEEL DDSLLEDDE
//

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