ID V2YII1_9FIRM Unreviewed; 837 AA.
AC V2YII1;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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 Synonyms=gyrA_1 {ECO:0000313|EMBL:USF27204.1};
GN ORFNames=N510_002150 {ECO:0000313|EMBL:USF27204.1}, N510_01050
GN {ECO:0000313|EMBL:ESL15016.1};
OS Firmicutes bacterium ASF500.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1378168 {ECO:0000313|EMBL:ESL15016.1};
RN [1] {ECO:0000313|EMBL:ESL15016.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF500 {ECO:0000313|EMBL:ESL15016.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF27204.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF500 {ECO:0000313|EMBL:USF27204.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01897}.
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DR EMBL; AYJP01000005; ESL15016.1; -; Genomic_DNA.
DR EMBL; CP097573; USF27204.1; -; Genomic_DNA.
DR AlphaFoldDB; V2YII1; -.
DR STRING; 1378168.N510_01050; -.
DR PATRIC; fig|1378168.3.peg.1096; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_9; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000017395; 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}; 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:UP000017395};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 22..477
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT COILED 442..469
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 133
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 837 AA; 94767 MW; BA3184CA6D175F00 CRC64;
MSKKPQYDPE EIRYPDQKII TSSLVPEMEN SYIEYAMSVI VGRALPDVRD GLKPVHRRIL
YAMYEDNLTA DKPFKKSATC VGDVLGRYHP HGDQSVYDAL VRLAQDFSMR YMLVDGHGNF
GSIDGDPPAA YRYTEARMSK LSDEMLRDIE KDTVDWDPNF DETRKEPKTL PSRFPNLLVN
GSSGIAVGMA TNIPPHNMRE VINAAICVLD DPEATLADLM EHIHGPDFPT RAIIMGRSGI
RAAYATGRGR VTIRARHEFE EFGKDRTRIV ITEIPYQVNK RMLIKSMADQ VEDKRLEGIS
DIRDETDRNG MRIVIELKRD ANPQVVLNRL FAQTQLQTTF AINMLALVEV NGKLQPRILS
LRHILDEYIA YQEQVIIRRT KYDLRKAQER AHLLEGLLIA QDNIDEVIHI IRNSYDNAKE
RLMERFGLDD VQAQAICDMR LIALQGLNRE KLEAEYKELE ERIAYFNELL ASETMLRGVL
KDELTAIRDK YGDDRVTEIQ DVEDEIDIED LIEEEQCVFT LTQAGYIKRT PVSEYAAQSK
GGMGKKGITT REEDYVVDVF TASTHDYILF FTDTGKVYRK KGYQIPESGK TAKGTNIINI
LQVEQGERVQ AMLHYREHEG EELYLFMVTR NGTVKRLPVQ TLKNLRNNGI RALRLDEGDQ
LVSVRETDGS KKILIATHDG MAVCFDENDV RPMGRDAVGV RGIRLREGDY VVGAARALEG
KTVLSITEKG FGKRTPVEEY RITNRGGLGI KNYMVTDKTG PIVGVKVVDG SEDLLVVTQA
GILIRTHVDA IKQCGRSTQG VIVMRFKEEG DKVISLALAE REENGETVQP EEAPAEE
//
