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Database: UniProt
Entry: A0A1G4WLL3_9MYCO
LinkDB: A0A1G4WLL3_9MYCO
Original site: A0A1G4WLL3_9MYCO 
ID   A0A1G4WLL3_9MYCO        Unreviewed;       834 AA.
AC   A0A1G4WLL3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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   ORFNames=SAMN02799620_03761 {ECO:0000313|EMBL:SCX24727.1};
OS   Mycolicibacterium fluoranthenivorans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=258505 {ECO:0000313|EMBL:SCX24727.1, ECO:0000313|Proteomes:UP000199707};
RN   [1] {ECO:0000313|Proteomes:UP000199707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UNC267MFSha1.1M11 {ECO:0000313|Proteomes:UP000199707};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FMUB01000007; SCX24727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4WLL3; -.
DR   STRING; 1502745.SAMN02799620_03761; -.
DR   Proteomes; UP000199707; Unassembled WGS sequence.
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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   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};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_01897}.
FT   DOMAIN          19..477
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          449..476
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOTIF           538..544
FT                   /note="GyrA-box"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT   ACT_SITE        130
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ   SEQUENCE   834 AA;  92511 MW;  50A531A4695019D6 CRC64;
     MTDTTLPPGD EAGDRIEPVD IQHEMQRSYI DYAMSVIVGR ALPEVRDGLK PVHRRVLYAM
     FDSGFRPDRG HAKSARSVAE TMGNYHPHGD SSIYDTLVRM AQPWSLRYPL VDGQGNFGSP
     GNDPAAAMRY TEARLTPLAM EMLREIDEET VDFIPNYDGR VQEPTVLPSR FPNLLANGSG
     GIAVGMATNI PPHNLNELAE AVYWCLENHE ADEEATLAAC CERVKGPDFP THGLIVGSQG
     INDTYTTGRG SIRMRGVVEI EEDSRGRTSI VITELPYQVN HDNFITSIAE QVRDAKLTGI
     SNIEDQSSDR VGLRIVVELK RDAVAKVVLN NLYKHTQLQT SFGANMLSIV DGVPRTLRLD
     QMIRYYVEHQ LDVIIRRTRY RLRKANERAH ILRGLVKALD ALDEVIALIR ASANADVARS
     GLMELLDVDE IQAQAILDMQ LRRLAALERQ RIVDDLAKIE AEIADLEDIL AKPERQRAIV
     RDELKEIVEK HGDERRTRII AADGDVTDED LIQREDVVVT ITETGYAKRT KTDLYRSQKR
     GGKGVQGAGL KQDDIVNHFF VCSTHDWILF FTTQGRVYRA KAYDLPEASR TARGQHVANL
     LAFQPEERIA QVIQIQSYED APYLVLATRN GLVKKSKLVD FDSNRSGGIV AVNLRDGDEL
     VGAVLCSAED DLLLVSANGQ SIRFSATDEA LRPMGRATSG VQGMRFNEDD RLLSLNVVRE
     GTYLLVATAG GYAKRTDIEE YTVQGRGGKG ILTIQYDRRR GSLVGALIVD DDTELYAITS
     GGGVIRTAAR QVRKAGRQTK GVRLMNLGEG DTLIAVARNA EGPEEPEDDE TPDE
//
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