ID A0A1U9NP62_9BACT Unreviewed; 868 AA.
AC A0A1U9NP62;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:AQT69508.1};
GN ORFNames=STSP2_02699 {ECO:0000313|EMBL:AQT69508.1};
OS Anaerohalosphaera lusitana.
OC Bacteria; Planctomycetota; Phycisphaerae; Sedimentisphaerales;
OC Anaerohalosphaeraceae; Anaerohalosphaera.
OX NCBI_TaxID=1936003 {ECO:0000313|EMBL:AQT69508.1, ECO:0000313|Proteomes:UP000189674};
RN [1] {ECO:0000313|Proteomes:UP000189674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST-NAGAB-D1 {ECO:0000313|Proteomes:UP000189674};
RA Spring S., Bunk B., Sproer C.;
RT "Comparative genomics and description of representatives of a novel lineage
RT of planctomycetes thriving in anoxic sediments.";
RL Submitted (FEB-2017) 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; CP019791; AQT69508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9NP62; -.
DR STRING; 1936003.STSP2_02699; -.
DR KEGG; alus:STSP2_02699; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000189674; 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:UP000189674};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 15..494
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 835..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 556..562
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 868 AA; 96942 MW; DB17EEBF97DB28D7 CRC64;
MADINETIND RFEDMKILDE MKTSYLNYAM SVIVSRALPD VRDGLKPSQR RILVAMNDLN
LGPRGKHRKC AKIVGDTSGN YHPHGDQATY GTLVRLGQHW NMRYTLVDPQ GNFGSIDADP
PAAMRYTEAR FASPAPDMME DIEKDTVDFV PNYDETRKEP VVLPSKFPNL LVNGASGIAV
GMATNIAPHN LNEVCDALLL MIDNPDCTFK DILEVLPGPD FPTGGIICGR KGILDAYVHG
RGHLKVRAKH HIEESKRGKI SIIFTEIPYM VVKATIVSKI ADCVREGTIP EISDVRDESD
RKGMRIVVEV RKDADENVVL NKLYRYTPLQ NTFAINNVAL VNSRPETLNI KQMLKLYIEH
RLIVIRRRTR YLLKKARNRA HILEGLILAV SDIDEIIELI KKSPDAPTAK INLMEKPLKL
VESETLRRLL PESFVSERHG KEQFLTGPQA DAILTMQLQR LTGLEIEKLA KEYGDLTEKI
EGYEALLSNK DMQFDVVRED IHEIKGKYGD DRRTNISEED LTGFDLEDLI TEEEVLVMIS
HQGYMKRMPI DTYRKQARGG RGIIGSSTKE DDFIEHLFTA STHDYLLVFT TGGICYWLKV
YNIPAMSRQS KGRNIANLLD LGDDSIASIL NVREFDDQRQ LLMATRNGIV KKTVLSAYGN
PRSNGVKAVR LDEGDWVIGV DVTSGENEII LGTEKGMTIR FHEADARSMG RVSRGVKGIS
LAKDDAVVGM VIVEEGASLL TACENGYGKR TALEEYRVQS RGGKGIINIK GLDRNGKVIA
IKAVQDEDDI MMITAQGMII RTGLEEVRVI GRSTSGVRMI NLKKDDKLVA VERLSLEEEE
EAAESAQNGE ESSSEAEGSA EPDENAEE
//
