ID A0A208Y7U6_9BURK Unreviewed; 877 AA.
AC A0A208Y7U6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=CDO44_02890 {ECO:0000313|EMBL:OVZ64328.1};
OS Pigmentiphaga sp. NML080357.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pigmentiphaga.
OX NCBI_TaxID=2008675 {ECO:0000313|EMBL:OVZ64328.1, ECO:0000313|Proteomes:UP000196551};
RN [1] {ECO:0000313|EMBL:OVZ64328.1, ECO:0000313|Proteomes:UP000196551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML080357 {ECO:0000313|EMBL:OVZ64328.1,
RC ECO:0000313|Proteomes:UP000196551};
RA Bernier A.-M., Bernard K.;
RT "Pigmentiphaga species Genome sequencing and assembly.";
RL Submitted (MAY-2017) 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:OVZ64328.1}.
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DR EMBL; NINW01000008; OVZ64328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A208Y7U6; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000196551; 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..506
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT REGION 849..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 571..577
FT /note="GyrA-box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
FT ACT_SITE 122
FT /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01897"
SQ SEQUENCE 877 AA; 97053 MW; E6CC5B7B963BDF02 CRC64;
MDSFAKETLP ISLEEEMRRS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMHELNNDWN
RAYKKSARIV GDVIGKYHPH GDQAVYDTIV RMAQPFSLRY MLVDGQGNFG SVDGDGAAAM
RYTEIRLAKI AHELLADIDQ ETVDFGPNYD GSEKEPLLLP TRLPNLLVNG SSGIAVGMAT
NIPPHNLAEV VDGCLYCLRN PACTVDELIE IIPAPDFPTG GIIYGMSGVR EGYRTGRGRV
VMRAKTHFED VEKGGREAIV VDEIPYQVNK RSLLERIAEL VNEKKIEGIS DIRDESDKDG
MRVVIELKRG EVPEVVLNNL YKNTQLQDTF GMNLVALVDG QPRLLNLKQM VEHFLAHRRE
VVTRRTVFQL RKARERGHVL EGLAVALANI DDFIAIIKAA PTPPIARQEL MARTWDSSLV
REMLARAEAE TAGGRDAYRP EGLPAEYGMQ DDGLYRLSDT QAQEILNMRL QRLTGLEQDK
IVGEYKDVMA NIADLLDILA KPERVTVIIG DELSAIKAEF GTDAKDTRRS HIELNATELD
TEDLITPTDM VVTLSHAGYI KSQPLSEYRA QKRGGRGKQA TATKEDDWID QLFIANTHDS
ILCFSNRGRV YWLKVWEVPQ GTRNSRGKPI VNMFPLSDGE KITVVLTVKA YSEDHYVFMA
TAKGTVKKTP LSEFSNPRKA GIIAVDLDEG DYLIGASLTD GKHDVMLFSD AGKAVRFDEN
DVRPMGRTAR GVRGMMLEDS HTVIALLVAE NETQSVLTAT ENGYGKRTPI GEYTRHGRGT
KGMIAIQTTE RNGKVVGAVL VDPSDEIMLI TTGGVLVRTR VSEIREMGRA TQGVTLINVD
EGTHLSGVQR VVESDTEEPE GGGADAEPEA PSSSEAE
//
