ID F3G7M7_PSESJ Unreviewed; 173 AA.
AC F3G7M7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=DNA topoisomerase IV subunit A {ECO:0000313|EMBL:EGH43077.1};
DE EC=5.99.1.- {ECO:0000313|EMBL:EGH43077.1};
DE Flags: Fragment;
GN ORFNames=PSYPI_12034 {ECO:0000313|EMBL:EGH43077.1};
OS Pseudomonas syringae pv. pisi str. 1704B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629263 {ECO:0000313|EMBL:EGH43077.1, ECO:0000313|Proteomes:UP000004986};
RN [1] {ECO:0000313|EMBL:EGH43077.1, ECO:0000313|Proteomes:UP000004986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1704B {ECO:0000313|EMBL:EGH43077.1,
RC ECO:0000313|Proteomes:UP000004986};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
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 -!- 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:EGH43077.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEAI01000599; EGH43077.1; -; Genomic_DNA.
DR AlphaFoldDB; F3G7M7; -.
DR HOGENOM; CLU_002977_3_0_6; -.
DR Proteomes; UP000004986; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR PANTHER; PTHR43493:SF1; DNA TOPOISOMERASE 4 SUBUNIT A; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:EGH43077.1};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 15..173
FT /note="DNA topoisomerase type IIA"
FT /evidence="ECO:0000259|SMART:SM00434"
FT NON_TER 173
FT /evidence="ECO:0000313|EMBL:EGH43077.1"
SQ SEQUENCE 173 AA; 19159 MW; AA60547A3329919E CRC64;
MSDSLDLSLD GVERRSLADF TEQAYLNYSM YVIMDRALPH IGDGLKPVQR RIIYAMSELG
LGADAKHKKS ARTVGDVLGK FHPHGDSACY EAMVLMAQPF SYRYTLVDGQ GNWGAPDDPK
SFAAMRYTEA RLSRYSEVLL SELGQGTADW VPNFDGTLDE PAVLPARLPN ILL
//
