ID A6ER35_9BACT Unreviewed; 840 AA.
AC A6ER35;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=SCB49_11012 {ECO:0000313|EMBL:EDM44116.1};
OS unidentified eubacterium SCB49.
OC Bacteria; Bacteroidota; environmental samples.
OX NCBI_TaxID=50743 {ECO:0000313|EMBL:EDM44116.1, ECO:0000313|Proteomes:UP000003659};
RN [1] {ECO:0000313|EMBL:EDM44116.1, ECO:0000313|Proteomes:UP000003659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCB49 {ECO:0000313|EMBL:EDM44116.1,
RC ECO:0000313|Proteomes:UP000003659};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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:EDM44116.1}.
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DR EMBL; ABCO01000005; EDM44116.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ER35; -.
DR STRING; 50743.SCB49_11012; -.
DR Proteomes; UP000003659; 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:UP000003659};
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 COILED 434..475
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 523..529
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 121
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 840 AA; 94188 MW; 8CBB85BC414B610E CRC64;
MADGEKLISI NIEDEMKSAY IDYSMSVIVS RALPDVRDGM KPVHRRVLFG MHELGIRATG
AHKKSARIVG EVLGKYHPHG DTSVYDAMVR MAQEWSLRYM LVDGQGNFGS IDGDSPAAMR
YTEARMQRIS EDMLADIDKE TVDHQLNFDD TLMEPKVLPT RIPGLLINGA SGIAVGMATN
MPPHNLTEVV NGTLAYIDDD EITIDGLMEH IKAPDFPTGG IIYGYDGVKD AFHTGRGRVV
MRAKASFEEV QGRECIIVSE IPYQVNKADM IKKTADLVNE KKIEGIANIR DESDRNGMRI
VYILKRDAIP NIVLNTLYKY TALQSSFSVN NIALVNGRPQ LLNLKELIHY FVEHRHEVVV
RRTEYLLRKA NERAHILEGL IIASDNIDEV IRLIRASANA DEARAALIEA FKLTEIQAKA
IVEMRLRQLT GLEQDKLRAE YEELMKTIAD YKDILANKER RMNIIKEELL EVQRKYGDDR
RSVIEYAGGD VSITDLIPDE QVVLTISHAG YIKRTSLTEY KTQNRGGVGQ KASATRNEDF
LEHLFVGTNH QYMLFFTQKG KCFWMRVFEI PEGSKTSKGR AIQNLINIEP DDKVMAFICT
QDLKDEEYVN SRYVIMATKK GQVKKTPLEQ YSRPRTNGIN AITIKDDDEL LEAKLTRGDS
QVMLAVKSGK AIRFEESKTR PMGRNASGVR GIRLADDNDE VVGMIAINDL ESEILVVSDK
GYGKRSSIED YRITNRGGKG VKTINVTEKT GQLVAIKNVI DSDDLMIINK SGIAIRMDVS
SLRVMGRATQ GVRLIKVRED DSIAAVAKVM KDENEVEDAE AVEVEGVEVD GTSLDSNEEE
//
