ID A0A2N0VES5_9BACT Unreviewed; 824 AA.
AC A0A2N0VES5;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=CWD77_14940 {ECO:0000313|EMBL:PKD42693.1};
OS Rhodohalobacter barkolensis.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae;
OC Rhodohalobacter.
OX NCBI_TaxID=2053187 {ECO:0000313|EMBL:PKD42693.1, ECO:0000313|Proteomes:UP000233398};
RN [1] {ECO:0000313|EMBL:PKD42693.1, ECO:0000313|Proteomes:UP000233398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=15182 {ECO:0000313|EMBL:PKD42693.1,
RC ECO:0000313|Proteomes:UP000233398};
RA Han S.;
RT "Rhodohalobacter 15182 sp. nov., isolated from a salt lake.";
RL Submitted (NOV-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}.
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:PKD42693.1}.
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DR EMBL; PISP01000006; PKD42693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N0VES5; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000233398; 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:UP000233398};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 9..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 523..529
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 120
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 824 AA; 92950 MW; 3309A8C9CDE4380E CRC64;
MATEKIIPIS IEDEMQSSYI DYSMSVIVSR ALPDVRDGLK PVHRRILYGM SDLGMLHNRN
FKKSARIVGE VLGKYHPHGD SAVYDSIVRM VQEFSLRYPL VNGQGNFGSI DGDSAAAMRY
TEVRMQRIAE ELLADINKET VDYQTNFDDT LTEPTVLPAM LPNLLLNGAS GIAVGMATNM
APHNITEVID GTVAVIDNPD IETEELMKHI TAPDFPTGGI IYGYEGVKEA YSTGRGKITM
RARANVEELR NSREQIVVTE IPYQVNKATL IQKVAQLVGD EKITEISEIR DESDREGMRI
VIILKRSANA GVVLNQLYKY TQMQQTFGVI NLALVKGRPK VMSLKELITR FIEHRVEVII
RRTIYDLDQA EARAHILEGL KIALDNLDEV IKTIRASKNP QEANEELRRK FALTDIQAKA
ILDMRLQKLT GLERDKIDTE YRDIASQISD YREILSNRDE QNEIIKKELL ELKGRYGDER
RTQIVYSADD FNIEDMIADE DVVVTISNKG FIKRMPVSGY RRQRRGGKGM KGTTTKDDEY
VEHLFVATNH NYILFFTEKG NCYWLKVYEI PEGSRLARGR AIVNLIDIEK DDSIKTFVPV
KTLDDEEYIK SHSIIMSTKQ GQVKKTSLEA YSRPRRDGII AINIKDDDSL LEAALTDGES
NIILANKSGR AIRFHEEEAR EMGRNTSGVR GMNLNKGDEL VDMVVIKNTH EATVLAISEN
GYGKRSLVDD YREQSRGGKG VITLKVTPKT GDLIALKEVS DKDDLMVITE RGKIIRMQCK
GIRTMGRNTQ GVRIMRLDED GKIAAVTRVV NEEETSEEDA PSVE
//
