ID A0A1I1A8T0_9CELL Unreviewed; 898 AA.
AC A0A1I1A8T0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN05421867_11613 {ECO:0000313|EMBL:SFB34355.1};
OS Cellulomonas marina.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=988821 {ECO:0000313|EMBL:SFB34355.1, ECO:0000313|Proteomes:UP000199012};
RN [1] {ECO:0000313|EMBL:SFB34355.1, ECO:0000313|Proteomes:UP000199012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6945 {ECO:0000313|EMBL:SFB34355.1,
RC ECO:0000313|Proteomes:UP000199012};
RA de Groot N.N.;
RL Submitted (OCT-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; FOKA01000016; SFB34355.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1A8T0; -.
DR STRING; 988821.SAMN05421867_11613; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000199012; 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:UP000199012};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 33..490
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 869..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 443..489
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 551..557
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 144
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 898 AA; 98936 MW; 9731C7435714E241 CRC64;
MTDTPDGPGG GTPENPLWQV GADGIAHGRI DQVDLQLEMQ RSYLDYAMSV IVGRALPDVR
DGLKPVHRRV LYAMYDGGYR PDRQFSKCSR VVGDVMGKFH PHGDGAIYDA LVRLVQDWSL
RYPLVAGQGN FGSPGDDPAA APRYTECRMA PLAMEMVRNI DEDTVDFQDN YDGREQEPVV
LPSRFPNLLV NGSAGIAVGM ATNIPPHNLR EVAAGVQWHL DHPDASKEEL LEALLERIKG
PDFPTAATIL GHRGIEEAYR TGRGSITMRA VVEVEEIQNR ICLVATELPY QVNPDRLAEK
IVELARDGRV QGIADVRDET SGRTGQRLVI VLKRDAVAKV VLNNLYKHTQ LQDTFGANML
ALVDGVPRTL SIDAFVRHWV THQIEVIRRR TQYRLADAER RIHIYRGYLK ALDALDEVIA
LIRASASADA ARTGLMELLD IDEEQANAIL QMQLRQLAAL ERQNILERYQ ELERLIAEYN
AILASEQRQR DIVSEELAEV VDRYGDERRT RVLPHDGEVS IEDLIAEEEV VVTITRGGYA
KRTRTDAYRA QRRGGKGVRG AQLRQDDLVD HFFTTTTHHW LLFFTNLGRV YRAKAYELPE
GGRDAKGQHV ANLLAFQPGE KIAQVLDLRG YDQAQYLLLA TQRGLVKKTR LSDYDTNRTG
GVIAINLRED EEGRADALVA ARLADPEQDV ILVSRKGQSV RFTASDEALR PMGRATSGVT
GMKFRGDDEL LAMDVVREDA DLFTVTQGGI AKRTALTVEN YRQQGRGGLG VRVANLPEAN
GDLVGALVVD PEDEVLVIME HGKIVRSAAA EVNATGRTTQ GVIFAKPDAG DRIIAVARNP
ERQAAEEVVV AEDLAPAADV EVVEADVTPV VEADGTEPAG SVEDDGTTGP DAADGRDA
//
