ID W0E165_MARPU Unreviewed; 867 AA.
AC W0E165;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=MARPU_04635 {ECO:0000313|EMBL:AHF03248.1};
OS Marichromatium purpuratum 984.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Marichromatium.
OX NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF03248.1, ECO:0000313|Proteomes:UP000005275};
RN [1] {ECO:0000313|EMBL:AHF03248.1, ECO:0000313|Proteomes:UP000005275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=984 {ECO:0000313|EMBL:AHF03248.1,
RC ECO:0000313|Proteomes:UP000005275};
RG DOE Joint Genome Institute;
RA Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) 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; CP007031; AHF03248.1; -; Genomic_DNA.
DR RefSeq; WP_005220266.1; NZ_CP007031.1.
DR AlphaFoldDB; W0E165; -.
DR STRING; 765910.MARPU_04635; -.
DR KEGG; mpur:MARPU_04635; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_6; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000005275; 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:UP000005275};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..501
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 845..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 562..568
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 867 AA; 96686 MW; 57EFADD52A7823CF CRC64;
MPEFAREVLP INLEDEMRQS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF SMHEQGNVWN
RAYRKSARVV GDVMGKYHPH GDSAIYDTMV RMAQPFSMRN LLVDGQGNFG SVDGDPPAAM
RYTEVRMTRI ADALLDDLDK ETVDFAPNYD NTEQEPTVLP ARFPNLLVNG SSGIAVGMAT
NIPPHNLNEV IDACLAIIDD PMVDLEQLIE LVPGPDFPTG ALINGVHGIR EAYRSGRGRV
VMRARADIEE QSRSGREAIV VTELPYQVNK ARLLERIAEL VKEKKIEGIA QDGLRDESDK
DGMRIVIELK RDTHPEVLLN NLYQHTQMQQ VFGINMVALV DGQPRTLNLK QILEYFLRHR
RDVVTRRTLY ELRKARDRAH VLEGYAIALA NIDEVIATIK ASPSPAEARE RLMMRAWAPG
AVSDMLSRTG AEQTRPETLD PGFGMTDEGY RLSERQAKAI LELQLHRLTG LEQEKILKEF
EEILARIGEL LAILGDPDRL MAVIREELEA IREQFGSARR TEIQVDHTDL TLEDLIAPED
LVVTLSHQGY VKAQPLSDYQ AQHRGGRGKS ATSFREEDFI DRLFVANTHD TVLCFSSRGR
VYWIKVYELP QGGRSARGRP MVNLLPLEQG ERITAMLPVR EYEDGYFVFM ATSAGTVKKT
PLRDFSRPLS RGIIAIDLHE DEYLVGVAIT DGDQDLMLFT SAGKAVRFSE DQVRAMGRTA
HGVRGVKLQP DQRVISLVVP EPGTVLSVTE NGYGKRTTVD QFPTKGRGTQ GVIAIRTSER
NGEQVGAVLV LPGDEIMLIT EHGTLIRTSV DEIPVVGRDA QGVKLINLGD GERLAYVERV
VALDEEEAEA DASDVADEAG ADAEPRD
//
