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Database: UniProt
Entry: A0A2T0SRB2_9BACT
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Original site: A0A2T0SRB2_9BACT 
ID   A0A2T0SRB2_9BACT        Unreviewed;       903 AA.
AC   A0A2T0SRB2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Topoisomerase-4 subunit A {ECO:0000313|EMBL:PRY35947.1};
GN   ORFNames=CLV58_11375 {ECO:0000313|EMBL:PRY35947.1};
OS   Spirosoma oryzae.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX   NCBI_TaxID=1469603 {ECO:0000313|EMBL:PRY35947.1, ECO:0000313|Proteomes:UP000238375};
RN   [1] {ECO:0000313|EMBL:PRY35947.1, ECO:0000313|Proteomes:UP000238375}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28354 {ECO:0000313|EMBL:PRY35947.1,
RC   ECO:0000313|Proteomes:UP000238375};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC       family. {ECO:0000256|ARBA:ARBA00008263}.
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:PRY35947.1}.
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DR   EMBL; PVTE01000013; PRY35947.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0SRB2; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000238375; 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; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
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   PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:PRY35947.1};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          51..492
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          881..903
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          464..491
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        17..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   903 AA;  101981 MW;  6705CA762D35CF5E CRC64;
     MIDEENLDPM DESAEQPGDT TPANAEPLST TEPDGQSADS SPESQVLHDQ TVVSGLYENY
     FLDYASYVIL ERAVPAVEDG FKPVQRRILH ALREMDDGRF NKVANVIGQT MQYHPHGDAS
     IGEALVNIGQ KELLFDTQGS WGDVRTGDGA AAPRYIEVRL SKFAHDTVYN EKTTEWQLTY
     DGRKREPVTL PVKFPLLLAQ GVEGIAVGLS TKVLPHNFNE LIDASIQILK DKPVQLYPDF
     QTGGLIDVSN YNDGHRGGKV RVRARIEEVD KKTLAIRDVP YGVTTSQLID SIVKAAELGK
     IRIKAPSRNV AAVVDNTARD VEILVHLQPG VSPDVTIDAL YAFTDCEVSI SPNACVIIGD
     KPHFVSVTDI LKVNTHQTVS LLQRELEIRR SELMERLLYS SLEKIFIENR IYRKIEECET
     FEAVLQTIDK ALKPFKKQFY REIVEDDLIR LTEIKIKRIS KYDGFKAEEL MRKLEQELAE
     VEDNLANLTR YAIAYFKDLQ KKYGKGRERK TEIRGFNTIA ASVVAAANQK LYVDRENGFI
     GYGLKKDEYV SDCSDIDDVI VFRRDGVCMV SKVQDKVFVG KDIIYVSVFK KNDERKIYNL
     VYLDAKSGIS MIKRFPITGV TRDREYDLTM GSPKSKITYF SANENGEAEV ITVNLTAQSS
     AKIKQFDYDF ASVGIKNRSA QGNILTKYPV RKITQKSGGV STLGGVDIWY DEHLGRLNRD
     ERGRLLGKFD AKDSILVIYK DGQYELTSFD LTNRYEPNEI QSLSRFEPET VVSAVYYEAN
     QKAWYVKRFK VETTTLDKKF SFIGDVKGSK NLAVTTDRYP RIEIVHQVKD RGPVEKMVLE
     PEGFIEIRGW KALGNKLPFA RVKDVKLLEP KVVKEAPAAV REPELVETDE PEPKETAQLG
     LFS
//
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