ID F3ZQ73_9BACE Unreviewed; 859 AA.
AC F3ZQ73;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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=Bcop_1546 {ECO:0000313|EMBL:EGJ71739.1};
OS Bacteroides coprosuis DSM 18011.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ71739.1, ECO:0000313|Proteomes:UP000018439};
RN [1] {ECO:0000313|EMBL:EGJ71739.1, ECO:0000313|Proteomes:UP000018439}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ71739.1,
RC ECO:0000313|Proteomes:UP000018439};
RX PubMed=21677860; DOI=10.4056/sigs.1784330;
RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT strain (PC139).";
RL Stand. Genomic Sci. 4:233-243(2011).
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; CM001167; EGJ71739.1; -; Genomic_DNA.
DR RefSeq; WP_006744896.1; NZ_CM001167.1.
DR AlphaFoldDB; F3ZQ73; -.
DR STRING; 679937.Bcop_1546; -.
DR eggNOG; COG0188; Bacteria.
DR HOGENOM; CLU_002977_6_1_10; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000018439; 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}; Reference proteome {ECO:0000313|Proteomes:UP000018439};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 10..462
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 819..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 523..529
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 819..839
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 859 AA; 97098 MW; 31B03746FBC7E447 CRC64;
MVEQDRIIKI NIEDEMKSSY IDYSMSVIVS RALPDVKDGF KPVHRRILYG MMELGNTSDK
PYKKSARIVG EVLGKYHPHG DSSVYLAMVR MAQEWAMRYP LVDGQGNFGS VDGDSPAAMR
YTEARLNKMG EEMMQDLYKE TVDFDPNFDN TLQEPKVLPA RIPNLLVNGA SGIAVGMATN
MPPHNLSEVI DACQAYLENT EIDVEGLMQY VKAPDFPTGG FIYGMSGVKE AFETGRGRVV
MRARAEIEAG QTHEKIVISE IPYNVNKADL IKHIADLVNE KRIEGIANVN DESDRSGMRI
VVDCKRDANA NVVLNKLYKM TALQSSFGVN NVALVDGRPH TLNLRDLVAN FVEHRHDVVI
RRTQFDLRKA EERAHILEGL IIASDNIDEV IKIIRAAKNP NEAITNLMTR FELSEIQARA
IVEMRLRQLT GLMQDQLHGE YQEVMARIAE YKEILNNDEK CREVIKAELQ EVKDKYGDER
RSEIVYSSEE FNPEDFYSND PMIITISHMG YIKRTPLSDF TSQNRGGVGS KGTDTRDQDF
IEHIYPATMH NTMMFFTQMG KCYWLKVYEI PEGSKNSKGR AIQNLLNIDR NDAVNAYLRV
EDLNDEEFIN SHYVIFCTKH GVIKKTLLEQ YSRPRQNGVN AITIREDDKV IEVRLTNGKC
NIVIANKNGR AIRFHEENVR PMGRTATGVR GIRLDEDGQD EVVGMVAIRD LETETIMVVS
EEGYGKRSEV EDYRITNRGG KGVKTMNITE KTGKLVGIES VTDENDLMII NKSGVTIRLD
VEDVRVMGRA TQGVRLINLD KRNDHIGSIC KVLSEEEEEI IEEEDVDVEG MEQAPTEDED
TSTEGGNPST GMLFDDNDL
//
