ID A0A1I5MJ42_9BACT Unreviewed; 860 AA.
AC A0A1I5MJ42;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN04515674_101333 {ECO:0000313|EMBL:SFP09602.1};
OS Pseudarcicella hirudinis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Pseudarcicella.
OX NCBI_TaxID=1079859 {ECO:0000313|EMBL:SFP09602.1, ECO:0000313|Proteomes:UP000199306};
RN [1] {ECO:0000313|EMBL:SFP09602.1, ECO:0000313|Proteomes:UP000199306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E92,LMG 26720,CCM 7988 {ECO:0000313|Proteomes:UP000199306};
RA de Groot N.N.;
RL Submitted (OCT-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; FOXH01000001; SFP09602.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5MJ42; -.
DR STRING; 1079859.SAMN04515674_101333; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000199306; 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:UP000199306};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW Rule:MF_01897}.
FT DOMAIN 10..463
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 831..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..851
FT /note="Polar 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 860 AA; 96380 MW; 66C2B6352C583CAD CRC64;
MSENSNIIPI NIEDEMRGAY IDYSMSVIVS RALPDVRDGM KPVHRRVLFG MEELGVNYNK
AYKKSARIVG EVMGKYHPHG DASVYDTMVR MAQEWSLRYP LVDGQGNFGS IDGDFPAAMR
YTEARLKRIA EELLGDLNKE TVDFQPNFDD SLQEPTVLPA KIPNLLLNGT SGIAVGMATN
MAPHNLTEVI NGIIAYIDNR DITILELMEY IKAPDFPTGG TIYGIQGIKN AFETGRGRVV
VRGNATFETS KTGKDQIIVS EIPYMVNKSS LIKHCADLVN DKKIEGISEI RDESDRQGMR
IVFDLKRDAV PNVVLNNLYK YSALQSSFSV NNVALVKGRP MTLNLKDLIY HYVEHRNEVI
VRRTQYDLRE AQKRAHILEG FIIALDHLDA VIKLIRESRD PATAQQGLMA SFGLSEIQAK
AILEMRLQRL TGMERDKILS EYNEIKLLIS ELEDILAKPE RQLQIIKDEL ADVRARYGDE
RRTQINMTDD EFSVEDMIAD DEMLITISAQ GYIKRTPITE YRAQSRGGVG SRAVATKDDD
FTEHLFTATM HNWLLFFTER GKCFWLRVYA VPEGSKNSKG RPIQNLMNIE SGDSIRAVIN
VKSITDPDYI NNNFIVMCTE DGTIKKTTLE AYSRPRQNGI IAITIREGDR LLDVSLTNGN
NHIVIATNTG RSVRFEENRV RPMGRSAAGV KGIWIDEDIT TEKAIGMVCI ENPDTQQLLV
VSEKGFGKRS EVEDYRLTNR GGKGVKALNI TDKTGNLVAI KEVNDNNDLM IITKAGILIR
IAVADLRVMG RNTQGVKLIR LKNESDEISS VTKIDKEPDE VSEDVIVDEA IVQSGDSTEQ
EGGNTQEPLT EEAGEDNPEE
//
