ID A0A133Z8I5_9BACT Unreviewed; 866 AA.
AC A0A133Z8I5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=HMPREF1870_00041 {ECO:0000313|EMBL:KXB51753.1};
OS Bacteroidales bacterium KA00344.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1497954 {ECO:0000313|EMBL:KXB51753.1, ECO:0000313|Proteomes:UP000070254};
RN [1] {ECO:0000313|Proteomes:UP000070254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA00344 {ECO:0000313|Proteomes:UP000070254};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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:KXB51753.1}.
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DR EMBL; LSCT01000007; KXB51753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133Z8I5; -.
DR STRING; 1497954.HMPREF1870_00041; -.
DR PATRIC; fig|1497954.3.peg.39; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000070254; 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:UP000070254};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 15..474
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 833..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 446..494
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 535..541
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 126
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 866 AA; 97179 MW; B7D5B4A8623E966F CRC64;
MDENQTIDRD RILKINIEEE MKSSYIDYSM SVIVARALPD VRDGFKPVHR RILYGMLGLG
NTSDKPYKKC ARVVGEVLGK YHPHGDSSVY GALVRMGQDW NMRYKLVDGQ GNFGSVDGDS
PAAMRYTECR LAKMGEHIMD DIDKDTVDMT NNFDDTLKEP AVMPTKIPNL LVNGGNGIAV
GMATNMPTHN LGEVIDGCCA FIDNPDIDTE GLMEYIPAPD FPTGAYIYGI QGVKDAYNTG
RGRVVMRAKA EIETDENHDR IVVTEIPYGV NKQQLIEYIA ELVKEGRLEG ISNVNDESGR
QGMRIVVDVK RDANARVILN KLFKMTALQS SFSVNNIALI PNPKDPSLLR PKLLTLRECI
SYFIEHRHEV TIRRTKFDLN KAQERAHILE GLIIACDNID EVVHIIRGSK TPAEAQANLE
KRFELDNLQS KAIVDMRLSQ LTGLRMDQLH AEYEDLMKLI DELQSILDDP EKCKQVMKAE
LQEVKEKYGD ERRTQIILDE HEFNAEDFYP NDPVVITVSH LGYIKRTPLS DFREQARGGV
GSKGAQTRDK DFTEYIYPAT MHQIMMFFTK KGRCYWLHCY DIPEGDKTSK GRAIQNLLNI
DPDDAVNAFL RLRGRGFEDE EFVDSHYVVF ATKNGTVKKT SLREYSRPRA NGVIAINIVE
GDEVVDVRLT NGNNELILAD RNGRAVRFDE NTIRPMGRVA TGVRGMRIDD DDDAVVGMIV
VDDAEAETVM VVSEEGYGKR SDVEEYRKTN RGGKGVKTMA ITEKTGRLVA IKNVTDANDL
MIINKSGIVI RLAVAEVRVM GRATQGVRLI NLTKKNDTIA SVCKVMSSEL EAALEEEKVQ
DEDGTNGQSA ESPHKSEAST EDRNDE
//
