ID A0A2K4GDP9_9PSED Unreviewed; 889 AA.
AC A0A2K4GDP9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=C1886_04210 {ECO:0000313|EMBL:POA21786.1};
OS Pseudomonas sp. FW300-N1A1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2075555 {ECO:0000313|EMBL:POA21786.1, ECO:0000313|Proteomes:UP000236411};
RN [1] {ECO:0000313|EMBL:POA21786.1, ECO:0000313|Proteomes:UP000236411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW300-N1A1 {ECO:0000313|EMBL:POA21786.1,
RC ECO:0000313|Proteomes:UP000236411};
RA Spencer S.J., Aaring A.B., Hendricks A., Penterman J., Chakraborty R.,
RA Alm E.J.;
RT "Whole genome sequencing of deep branching strains shows evolution and
RT exchange across a contaminated watershed.";
RL Submitted (JAN-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 type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263, ECO:0000256|HAMAP-
CC Rule:MF_01897}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POA21786.1}.
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DR EMBL; PPSF01000005; POA21786.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4GDP9; -.
DR Proteomes; UP000236411; 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 841..889
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 845..859
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 889 AA; 98252 MW; AAF8940CE43E8DFD CRC64;
MGELAKEILP VNIEDELKQS YLDYAMSVIV GRALPDARDG LKPVHRRVLF AMSELGNDFN
KPYKKSARVV GDVIGKYHPH GDTAVYDTIV RMAQPFSLRY LLVDGQGNFG SVDGDNAAAM
RYTEVRMTKL AHELLADLHK ETVDWVPNYD GTEMIPAVMP TRIPNLLVNG SSGIAVGMAT
NIPPHNLGEV IDGCLALIDN PELTVDELMQ YIPGPDFPTA AIINGRAGII EAYRTGRGRI
YMRARSMIED IDKVGGRQQI VITELPYQLN KARLIEKIAE LVKEKKLEGI TELRDESDKD
GMRVVIELRR GEVPEVILNN LYAQTQLQAV FGINIVALID GRPRILNLKD LLEAFVRHRR
EVVTRRTVFE LRKARERGHI LEGQAVALSN IDPVIALIKA SPTPSEAKEA LVSTPWESSA
VVAMVERAGA DSCRPENLDP QYGLREGKYF LSPEQAQAIL ELRLHRLTGL EHEKLLAEYQ
EILNQIGELI RILNSATRLM EVIREELEVI RAEYGDVRRT EILDARLDLT LGDMIPEEER
VVTISHGGYA KTQPLAAYQA QRRGGKGKSA TGVKDEDYIA HLLVANSHTT LLLFSSKGKV
YWLKTYEIPE ASRAARGRPL VNLLPLDDGE YITTMLPVEE YTEGHYIFMA TANGTVKKTP
LESFSRQRSV GLIALELDEG DVLISAAITD GEREVMLFSD GGKVTRFKES DVRAMGRTAR
GVRGMRLPEG QKLISMLIPE EGSQILTASE RGFGKRTAIT EFPEYKRGGQ GVIAMVSNDR
NGRLVGAVQV LDGEEIMLIS DQGTLVRTRV DEVSSLGRNT QGVTLIKLAG DETLVGLERV
QEPSEVEGEE LEGEEGAELD GVVLDAGAEP DDGVESQQAD AADEEEPQD
//
