ID A0A1C3PHB0_9ACTN Unreviewed; 838 AA.
AC A0A1C3PHB0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, 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:SBW29189.1};
GN ORFNames=FDG2_6572 {ECO:0000313|EMBL:SBW29189.1};
OS Candidatus Protofrankia californiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae;
OC Protofrankia.
OX NCBI_TaxID=1839754 {ECO:0000313|EMBL:SBW29189.1, ECO:0000313|Proteomes:UP000199013};
RN [1] {ECO:0000313|Proteomes:UP000199013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wibberg D.;
RL Submitted (FEB-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; FLUV01002737; SBW29189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C3PHB0; -.
DR Proteomes; UP000199013; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199013};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 16..473
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 816..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 534..540
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 127
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 838 AA; 92420 MW; 7ABFCB7DA475BBB8 CRC64;
MTDVLPPPPG DRVEPIGIEV EMQRSYLDYA MSVIVGRALP EVRDGLKPVH RRVLYAMYDG
GYRPDRGYFK CSRVVGDVMG NYHPHGDSAI YDTLVRLAQP WSLRYPLVDG NGNFGSPGND
PPAAMRYTES RLAPLAMEML RDIDQDTVDF APNYDGRSQE PTILPSRFPN LLVNGAGGIA
VGMATNIPPH NLREVAGGVK WFLAHPDASD SELLDALLEM IKGPDFPTSG LIVGRQGIED
AYRTGRGSIR MRAVVQVEEN KGRTQLVVTE LPYQVNPDNL AEKIAELVRD NRISGISDIR
DETSARTGQR LIIDLKRDAV AKVVLNNLYK HTQLQDTFGV NMLAIVDGVP RTLRLDQMVR
YYVDHQVDVI VRRTRYQLRK ARERLHVLEG LLIALDHLDE VITLIRNAES ADAARGQLMD
RFSLSEIQAV AILDMQLRRL AALERQKIID EAAELRAKIS ELEAILASPI RQREIIGEEL
TEIVDRFGDE RRTRLVPFEG DMSVEDLIAR EDVVVTVTRG GYAKRTKTDL YRSQRRGGKG
VQGAALREDD IVEHFFVTTT HHWLLFFTNK GRVYRAKAHE LPEQARTAKG QHVANILAFG
QDERIAEVMA IKDYHAAPYL VLATRRGLCK KTALAEFDSN RSGGLVAINL RDDDELIAAR
LVSAGDDLLL VSRQAQSIRF HADDEQLRPM GRATSGVIGM RFDTDDELLA MEVVPPDSDA
NLLVATSGGY AKRTSLGEYP VQGRGGKGVL TAKIVSTRGG LVGALVVGPD DQLYAITSNG
GVLRTVARDV RRAQRQTMGV RLIDLESSVQ VVGVARNADA EDNASNGSTA GPGGGDPA
//
