ID A0A1G8AAI9_9PSED Unreviewed; 921 AA.
AC A0A1G8AAI9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN05216603_106232 {ECO:0000313|EMBL:SDH17897.1};
OS Pseudomonas benzenivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=556533 {ECO:0000313|EMBL:SDH17897.1, ECO:0000313|Proteomes:UP000199168};
RN [1] {ECO:0000313|Proteomes:UP000199168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8628 {ECO:0000313|Proteomes:UP000199168};
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 type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC Rule:MF_01897}.
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DR EMBL; FNCT01000006; SDH17897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8AAI9; -.
DR STRING; 556533.SAMN05216603_106232; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000199168; 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}; 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 11..500
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 887..921
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 892..921
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 921 AA; 100937 MW; 02C16EA9A5F3A52D CRC64;
MGELAKEILP VNIEDELKQS YLDYAMSVIV GRALPDARDG LKPVHRRVLF AMSELGNDWN
KAYKKSARVV GDVIGKYHPH GDTAVYDTIV RMAQPFSLRY LLVDGQGNFG SVDGDNAAAM
RYTEVRMTKL AHELLADLHK ETVDWVPNYD GTEMIPAVMP TKIPNLLVNG SSGIAVGMAT
NIPPHNLGEV VDGCLALIDN PELTVDELMR YIPGPDFPTA AIINGRAGII EAYRTGRGRI
YIRARAEVED IDKVGGRQQI VVTELPYQLN KARLIEKIAE LVKEKKLEGI TELRDESDKD
GMRVVIELRR GEVPEVILNN LYAQTQMQSV FGINVVALID GQPKVLNLKD MLEAFIRHRR
EVVTRRTVFE LRKARERGHI LEGQAVALSN IDPVIALIKA SPSPAEAKEA LVSTAWESTA
VEAMVERAGA DACRPEDLDP QYGLRDGKYY LSPEQAQAIL DLRLHRLTGL EHEKLLAEYQ
EILAQIGELI RILTSSVRLM EVIREELEAV KAEFGDKRRT EILDARLDLT LGDLITEEER
VVTISHTGYA KSQPLSAYQA QRRGGKGKSA TGIKDEDYIA HLLVANSHST LLLFSSKGKV
YWLKTYEIPE ASRAARGRPL VNLLPLDEGE YITTMLQIDL EALQQSAGDD EELDDAEDAV
IEGEVLEADD GVEVAEAEEI DGETAELVAE PTGAYIFMAT AFGTVKRAPL AQFSRPRSSG
LIALKLKEGD TLIAAAITDG SKEVMLFSEA GKVIRFAESA VKVRNRVAGG IRGMKLGKGM
QLISMLIPES GAQILTASER GFGKRTPLSK FPRRGRGGQG VIAMVSNERN GKLVGAVQVL
DGEEIMLISD QGTLVRTRVS EVSSLGRNTQ GVTLIKLAKD ETLVGLERVQ EPSEEEGEEL
ETEGGEVAGE EAGGEDQAGE E
//
