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Database: UniProt
Entry: A0A385Z4V0_9PSED
LinkDB: A0A385Z4V0_9PSED
Original site: A0A385Z4V0_9PSED 
ID   A0A385Z4V0_9PSED        Unreviewed;       920 AA.
AC   A0A385Z4V0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   ECO:0000313|EMBL:AYC33560.1};
GN   ORFNames=D3880_14880 {ECO:0000313|EMBL:AYC33560.1};
OS   Pseudomonas cavernae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2320867 {ECO:0000313|EMBL:AYC33560.1, ECO:0000313|Proteomes:UP000265560};
RN   [1] {ECO:0000313|Proteomes:UP000265560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K2W31S-8 {ECO:0000313|Proteomes:UP000265560};
RA   Zhu H.;
RL   Submitted (SEP-2018) 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|ARBA:ARBA00000185,
CC         ECO:0000256|HAMAP-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}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263}.
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DR   EMBL; CP032419; AYC33560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A385Z4V0; -.
DR   KEGG; pcav:D3880_14880; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000265560; 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; 3.30.1360.40; -; 1.
DR   Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 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   NCBIfam; TIGR01063; gyrA; 1.
DR   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC/MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01897}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01897};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01897};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01897};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01897}; Reference proteome {ECO:0000313|Proteomes:UP000265560};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_01897}.
FT   DOMAIN          11..500
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          666..686
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          883..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           561..567
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   COMPBIAS        666..683
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        122
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   920 AA;  101795 MW;  7F24AE0C0E20E908 CRC64;
     MGELAKEILP VNIEDELKQS YLDYAMSVIV GRALPDARDG LKPVHRRVLF AMSELGNDWN
     KPYKKSARVV GDVIGKYHPH GDTAVYDTIV RMAQPFSLRY LLVDGQGNFG SVDGDNAAAM
     RYTEVRMAKL AHELLADLDK ETVDWVPNYD GTEQIPAVMP TKIPNLLVNG SSGIAVGMAT
     NIPPHNLREV IDGCLALIDN PELTVDELMQ YIPGPDFPTA GIINGRAGII EAYRTGRGRI
     YMRARAEIED IDKVGGRQQI IVTELPYQLN KARLIEKIAE LVKEKKLEGI TELRDESDKD
     GMRVVIELRR GEVGEVVLNN LYAQTQMQSV FGINVVALVD GQPRTLNLKD MLEVFVRHRR
     EVVTRRTVYE LRKARERGHI LEGQAVALSN IDPVIELIKT SPTPAEAKER LIATAWESSA
     VESMVERAGA EACRPEDLDP QFGLREGKYY LSPDQAQAIL ELRLHRLTGL EHEKLLTEYQ
     EILTQIGELI RILTNPLRLM EVIREELEQV KADFGDDRRT EIVASQVDLT IADLITEEER
     VVTISHGGYA KSQPLAAYQA QRRGGKGKSA TGVKDEDYIE HLLVANSHAT LLLFSSKGKV
     YWLRTFEIPE ASRTARGRPM VNLLPLDEGE RITAMLQVDL EALRQQALEG EEQDDIEGVL
     VEQDEVEDLA DDEDGDEAEG AEDKDETTGA YIFMATANGT VKKTPLVQFS KPRSSGLIAL
     RLEEGDTLIA AAVTDGAREV MMFSDGGKVI RFKESKVRTM GRTARGVRGM RLAEGQHIIS
     MLIPEQGAQI LTASERGYGK RTAMDEFPKR GRGGQGVIAM VSNERNGRLV GAIQVLDGEE
     IMLISDQGTL VRTRVDEVSS LSRNTQGVTL IKLASDETLV GLERVQEPSE VEGDDLEGDE
     SREAGEVAVE VVPEVPAGEE
//
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