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Database: UniProt
Entry: A0A1V2Q8U2_9PSEU
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ID   A0A1V2Q8U2_9PSEU        Unreviewed;      1139 AA.
AC   A0A1V2Q8U2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=ALI22I_29195 {ECO:0000313|EMBL:ONI84623.1};
OS   Saccharothrix sp. ALI-22-I.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1933778 {ECO:0000313|EMBL:ONI84623.1, ECO:0000313|Proteomes:UP000188617};
RN   [1] {ECO:0000313|EMBL:ONI84623.1, ECO:0000313|Proteomes:UP000188617}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ALI-22-I {ECO:0000313|EMBL:ONI84623.1,
RC   ECO:0000313|Proteomes:UP000188617};
RX   PubMed=28087533;
RA   Yeager C.M., Gallegos-Graves V., Dunbar J., Hesse C.N., Daligault H.,
RA   Kuske C.R.;
RT   "Polysaccharide degradation capability of Actinomycetales soil isolates
RT   from a semi-arid grassland of the Colorado Plateau.";
RL   Appl. Environ. Microbiol. 0:0-0(2017).
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:ONI84623.1}.
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DR   EMBL; MTQP01000066; ONI84623.1; -; Genomic_DNA.
DR   RefSeq; WP_077008782.1; NZ_MTQP01000066.1.
DR   AlphaFoldDB; A0A1V2Q8U2; -.
DR   STRING; 1933778.ALI22I_29195; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000188617; 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:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00081; Hint; 1.
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; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 2.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   InterPro; IPR006691; GyrA/parC_rep.
DR   InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR030934; Intein_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; TIGR01443; intein_Cterm; 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; 2.
DR   Pfam; PF00521; DNA_topoisoIV; 2.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 2.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ONI84623.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000188617};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          378..401
FT                   /note="Intein C-terminal splicing"
FT                   /evidence="ECO:0000259|PROSITE:PS50818"
FT   REGION          1101..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1113..1139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1139 AA;  122676 MW;  3CC2D720E15BD8CA CRC64;
     MARRKTPITR VDPSAFDRAG AQVFDNSLTT EIEDSYLEYA YSVIHSRALP DARDGLKPVH
     RRILFSMNEQ GYRPTSAYVK SSRVVGDCFV RGALVSTPEG LRPIEQIEIG DHVLDGRGEP
     VAVNAVYENP VSELVRVTWS DGHSMLVTPG QRFRTLDSTD ADVWTDARDL VGAHTVGFAG
     ERHANLLTDG DATGFVLGLV AAAGDVLPDG RVRLELADVD PIDIAHGWAI SNDLTASRDK
     IQANDHDRHT LTFAHHPDLD AAVSGRLDAV LRDRSAWTPF LAGLFTASGS VRDGREIVIP
     GGEPEYALLA DAGIRAHRDA TTLTITGRDA AALAVALLRW TGVGPRQDGL VQAIRNAKHA
     TDQPFPHVIS VEPATPDTTY DIQVASEEHA FVVSGFVVHN CMGKYHPHGD TAIYDAMVRL
     AQDFSLNTPL VDGHGNFGSP DDGPAASRYT EARMSPAAML LVGELDEDTV DFRPNYDGSL
     QEPSVLPAAF PNLLVNGTSG IAVGMATNMI PHNLGEVVAA ARHLVTHPDA TLDKLMEFIP
     GPDLPTGGVL LGLDEVRKAY ETGRGVVRMR AKVETGLLEG SRGRQAITVT ELPYGVGPEK
     IIEKITDEVT KSKRLSGISD VKDLTDRENG TRVVIECKVG VNPQALLADL YRLTPMEQSF
     GINNLVLVEG QPRTLGLKAL LEVFLKHRYE VVTRRTRYRR RKREDRLHLV EGLLRALLDI
     DKVIKLIRGS ENAAAAKEGL MKSFKLSEIQ ATYILDTPLR RLTRYDSLEL EAEQEKLRGE
     IAELSKILDD PAVLKKVVST ELGKVAKDLQ QERRTMLLDG DLKEVLAASK PAGPLEVADD
     PCQVVLSATG LVARTAAESE ESSEARRRNG RTKHDAVAAT VHTTARGQVL LVTNRGRAFK
     TDVLPLPVLP EQSGTVSLSG GMAASELVDL EAGEKVVGIA PLTDTESPGL ALGTRSGTVK
     VCSPEWPVRS DEFEVITLKE GDEVVGATWL AGADETLVFV TSEASLLRYP ASLVRPQGLR
     GGGMAGINVG SDSHVVFFGA VRTDDDVHGE PMVVTSTGQS VKVTPFSVYP AKGRATGGVR
     AHRFLKGETA LALAWVGPRP AGAAANGSPV ELPAPDERRD GSGHAHPGPD VVGHRIERD
//
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