ID A0A1V1W011_9ACTN Unreviewed; 919 AA.
AC A0A1V1W011;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=PD653_1047 {ECO:0000313|EMBL:GAW53646.1};
OS Nocardioides sp. PD653.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=393303 {ECO:0000313|EMBL:GAW53646.1, ECO:0000313|Proteomes:UP000194147};
RN [1] {ECO:0000313|Proteomes:UP000194147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD653 {ECO:0000313|Proteomes:UP000194147};
RA Ito K., Takagi K., Tanaka N., Kanesaki Y., Iwasaki A.;
RT "Nocardioides sp. PD653 draft genome sequence.";
RL Submitted (NOV-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}.
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:GAW53646.1}.
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DR EMBL; BDJG01000011; GAW53646.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1W011; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000194147; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW 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:UP000194147};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 23..481
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 859..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 453..480
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 542..548
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 134
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 919 AA; 100139 MW; 44E2ECAD95FD9CBA CRC64;
MTETPTDGGT TPPPGPGGRI EPVELKTSMQ RAYIDYAMAV IVGRALPDVR DGLKPVHRRV
LYAMYDGGYR PDRGFSKCSR VVGDVMGQYH PHGDTAIYDT LVRLAQPWVM RAPLVQGQGN
FGSPGNDSAA AMRYTECRMA PLALEMVRDI TEDTVDFQPN YDGRSSEPTV LPARYPNLLV
NGSAGIAVGM ATNIPPHNLR EVAAGAQWAL EHPDASREEL QDALIERIKG PDFPNGALIV
GREGIEQAYR TGRGSVTQRA IIEIDEDSRG RTCLSITELP YMVNPDNLAL KIAELADSGK
VQGISDVRDD SSGRTGQRLV VVLRRDAVAR VVLNNLLKHT ELQTNFSANM LALVDGVPRT
LTIDQFISNW VSHQIEVIQR RTRFRLAEAE RRAHVLRGLV KALDQLDEVI ALIRRSPEVD
DAREGLIALL EIDEIQANAI LDMQLRRLAA LERQKIIDQL AEIELEIADL EDILANEVRQ
RQIIGEELAA IVEKYGDDRR TQIIAADGDL SMEDLIPDED LVVSITRGGY AKRTRADQYR
TQKRGGKGVR GASLRGDDVV EHFISTTNHH WLLFFTTAGR VYRTKAYNLP EASRDAKGGH
VAGLLSFQPD ENIAQVLAIR DYEQAPYLVL ATRNGLVKKT RLGDYNSPRQ AGVIAINFRE
DDDVLIGAEL VNAEDDILLV SRKGQAIRFR ADDGQLRPMG RATSGVTGMK FRGDDSVLSM
SVIRAAQVAA EAAAGLSEVN EDTADVEVSA EAAAEVKPQY VFTITDGGFA KRSRISEYRL
TNRGGLGVRA MALANEDRGG LVGAFIVEEG DEVLSITQNG QVVRSPINDQ FRATGRSTMG
VKFVTPKAGD AVAVVARSVE ARDEEDEVDE TAPEGGAETV SEVGESSDEG TDATIEDAAD
SQAVTTDAEP DTDGESEGG
//
