ID A0A0U3CQZ5_9BURK Unreviewed; 881 AA.
AC A0A0U3CQZ5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:ALU90820.1};
GN ORFNames=Hrubri_3663 {ECO:0000313|EMBL:ALU90820.1};
OS Herbaspirillum rubrisubalbicans M1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1078773 {ECO:0000313|EMBL:ALU90820.1, ECO:0000313|Proteomes:UP000069903};
RN [1] {ECO:0000313|EMBL:ALU90820.1, ECO:0000313|Proteomes:UP000069903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1 {ECO:0000313|EMBL:ALU90820.1,
RC ECO:0000313|Proteomes:UP000069903};
RA Balsanelli E., Cardoso R.L.A., Cruz L.M., Faoro H., Chubatsu L.S.,
RA Muller-Santos M., Baura V.A., Huergo L.F., Wassem R., Broughton W.,
RA Monteiro R.A., Souza E.M., Pedrosa F.O.;
RT "Herbaspirillum rubrisubalbicans M1 complete genome.";
RL Submitted (DEC-2015) 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; CP013737; ALU90820.1; -; Genomic_DNA.
DR RefSeq; WP_058896557.1; NZ_CP013737.1.
DR AlphaFoldDB; A0A0U3CQZ5; -.
DR STRING; 1078773.Hrubri_3663; -.
DR KEGG; hrb:Hrubri_3663; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000069903; 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}; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..506
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT MOTIF 571..577
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 881 AA; 97583 MW; 79B60976F477C562 CRC64;
MDQFAKETIP ISLEEEMRKS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMHEMNNVWN
RPFVKCARVV GEVMGKYHPH GDASIYDTLV RMAQDFSLRY TLVDGQGNFG SIDGDGAAAM
RYTECRLDKI SNELLADIEK ETVDFVPNYD GKEKEPSVLP TRIPNLLVNG SSGIAVGMAT
NIPPHNITEV INGALHLLAN EHCTIDELIE LVPAPDFPTG GIIYGVSGVR DGYRTGRGRV
VMRAKTHFEE YGREGRIAII VDELPYQVNK KALLERIAEL VRDKKLEGIS DLRDESDKSG
MRVVIELKRG EVPEVVLNNL YKQTQLQDTF GMNMVALVDG QPRLLNLKQL LECFLSHRRE
VVTRRTVFEL RKARERGHVL EGLAVALANI DDFIAIIRAA PTPPIAKAEL MSKSWDSSMV
REMLARAGEA NEGGIEAFRP ESLPAHYGIQ SDGLYKLSDE QAQEILQMRL QRLTGLEQDK
IVNEYKDVMA QIADLLDILS KPARVTAIIT DELNAAKNDF GIGAKDERRS TIEHNATDLA
TEDLITPQDM VVTLSHTGYM KSQPVSEYRA QKRGGRGKQA MATKDDDWID QLFIANTHDY
ILCFSNRGRL YWLKVWEVPQ GSRNSRGKPI VNMFPLQDGE KITVILPVSG ANRSFPDDRY
VFMATSLGTV KKTPLSDFSN PRKAGIIAVD LDEGDFLIGA ALTDGQHDVM LFSDGGKAVR
FDENDVRPMG RTARGVRGMN LEETQQVIAL LVAENEQQSV LTATENGFGK RTPITEYTRH
GRGTKGMIAI QTSERNGKVV AATLVDSSDE IMLITTGGVL IRTRVSEIRE MGRATQGVTL
IAVEDGTKLS GLQRVVESDV EDVIESEGTE AAGGETPAAG E
//
