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
//