ID A0A1M5B7C6_9FLAO Unreviewed; 866 AA.
AC A0A1M5B7C6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=SAMN05443633_10456 {ECO:0000313|EMBL:SHF38092.1};
OS Chryseobacterium arachidis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1416778 {ECO:0000313|EMBL:SHF38092.1, ECO:0000313|Proteomes:UP000184518};
RN [1] {ECO:0000313|EMBL:SHF38092.1, ECO:0000313|Proteomes:UP000184518}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27619 {ECO:0000313|EMBL:SHF38092.1,
RC ECO:0000313|Proteomes:UP000184518};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01897}.
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DR EMBL; FQUT01000004; SHF38092.1; -; Genomic_DNA.
DR RefSeq; WP_072955953.1; NZ_FQUT01000004.1.
DR AlphaFoldDB; A0A1M5B7C6; -.
DR STRING; 1416778.SAMN05443633_10456; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000184518; 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};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 11..466
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 816..866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..866
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 866 AA; 97463 MW; B9816C5039D3ACF1 CRC64;
MQKEGERLIP INIVDEMKSS YIDYSMSVIV SRALPDVRDG LKPVHRRVLY GMYGLGVFSN
RKYLKSARIV GDVLGKYHPH GDSSVYDAMV RMAQDWSLRY PQVDGQGNFG SMDGDPPAAM
RYTEARLKKI SDEVLSDLDK ETVDFQNNFD DSLQEPTVLP SKIPNLLVNG TSGIAVGMAT
NMAPHNLTES VNAICAYIDN KEITIDELMQ HIIAPDFPTG GIIYGYDGVR DAFHTGRGRV
VLRAKVAFEE IGNRNAIIVN EVPYQVNKAE MIARTAELVK EEKIPGIYEI RDESDRRGLR
IVYELKNDAI PNVVLNLLYK YTALQTSFSV NNIALVHGRP EQLNLKDIIH HFVDHRHEVI
VRRTQYELRK AKERAHILEG FMKVIGTQDS LDRAISIIRH SANPQAAKEG LIEAFELSEI
QAQAILDLRL ARLTGMELDK IRDEYDAIMK EIADLEDILA NEPRRFQIIK DELIEIKEKY
GDERRTEIDY SGGEMSIEDI IPNESVVLTI SHAGYIKRTS LSEYKIQSRG GVGNKAATTR
DADFLEYIVS ATNHQYMLFF TEKGRCYWLR VFEIPEGSKT AKGRAVQNLI NIEPDDKIKA
YIRTNNLKDS EYVNQMSVVM VTKNGTIKKT SLEAYSRPRV NGVNAIEIRD NDQLLGAYLT
NGTSQIMIAT KNGKCIRFPE EKVREVGRGS IGVRGIAMED NDEVIGMIVV NDVENETVLV
VSEKGYGKRT AVEDYRITNR GGKGVITLNI TEKTGNLIAI QNVTDEDGLM IINKSGVAIR
MNMDEMRVMG RNTQGVRLIN LKKNDEIAAI AKVEMDKDVE EEEEDLEGNE EGVIGSLFDD
QENNTEAPQE ENENSSEETE NSDSEE
//
