ID A0A3M9NC85_9BACT Unreviewed; 879 AA.
AC A0A3M9NC85;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:RNI34883.1};
GN ORFNames=EFY79_14500 {ECO:0000313|EMBL:RNI34883.1};
OS Hanamia caeni.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Hanamia.
OX NCBI_TaxID=2294116 {ECO:0000313|EMBL:RNI34883.1, ECO:0000313|Proteomes:UP000267223};
RN [1] {ECO:0000313|EMBL:RNI34883.1, ECO:0000313|Proteomes:UP000267223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BO-59 {ECO:0000313|EMBL:RNI34883.1,
RC ECO:0000313|Proteomes:UP000267223};
RA Im W.T.;
RT "Draft genome sequence of Ferruginibacter sp. BO-59.";
RL Submitted (NOV-2018) 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:RNI34883.1}.
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DR EMBL; RJJR01000012; RNI34883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9NC85; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000267223; 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}; 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:UP000267223};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 21..475
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 823..879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 536..542
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT COMPBIAS 860..879
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 132
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 879 AA; 98715 MW; C3F9039C1843AC09 CRC64;
METTDEELPE SGAPRGRIIP VNIEEQMKSA YIDYSMSVIV GRALPDARDG LKPVHRRILY
GMYEMGNTYN KPHKKSARIV GDVMGKYHPH GDSSIYGTLV RMAQDWSMRY VLVDGHGNFG
SQDGDMPAAM RYTEVRLERI AETMLQDIEK DTIDWQLNYD DSDKEPSVLP TRIPQLLLNG
ASGIAVGMAT NILPHNLTEV VDACIAYVDN HEITIDELIK IVKAPDFPTG GIIYGYEGVK
QAMHTGRGRL VLRGKVNVET TNSGREKIII TEVPYQVNRD ALTEKIGYLI NEKVIDGVTD
VNNESNNKEG TRIVVDLKKD AISQVVINHL YKHTELQTSF GINNVALVKG RPHVLNIKEL
VSEFVNFRHE VVIRRTKFEL KKAEERAHIL EGFLIALDHL DEVIRLIRAA ATPDTAKDGL
MSEFKMSEIQ AKAVLELRLQ RLTGMERDKI REEHAQVMQT IANLKEILGD EGKRFQIIKE
ELTEIKEKYG DERKSEITYM ADEMSIEDLI EEEDVVVTIS HLGYIKRTSA TEFRQQRRGG
RGARGSKTRE EDYIEQLFIA STHHTLLFFT EKGRCFWLKV YEITEGDKQS KGRAIQNLIQ
IPSDDTVRTI ITIKNLQDTE YINNHYIVLC TRKGIIKKTK VTDFSRPRQN GINAITINEG
DQLLDACLTD GNQQIMMAVK SGRAIRFPEE KVRPTGRGAI GVFGISVDHE NDEVVGMICV
NISDPESSVL VVSAKGFGKR TAIEEYRITN RGGKGVKTIN VTEKTGDLIG LLNVKETQDL
MITCKSGVTI RTSIASIREA GRATQGVKLI KLDDGDEIAA ITKIDDHESE EEIEPVESLE
NENISSETDS SKEDAEPENQ IQNDESENSD NADDVSDNQ
//
