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Database: UniProt
Entry: A0A2A7MMV3_9CLOT
LinkDB: A0A2A7MMV3_9CLOT
Original site: A0A2A7MMV3_9CLOT 
ID   A0A2A7MMV3_9CLOT        Unreviewed;       963 AA.
AC   A0A2A7MMV3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   ORFNames=CQ394_11330 {ECO:0000313|EMBL:PEG32823.1};
OS   Clostridium neonatale.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=137838 {ECO:0000313|EMBL:PEG32823.1, ECO:0000313|Proteomes:UP000220840};
RN   [1] {ECO:0000313|EMBL:PEG32823.1, ECO:0000313|Proteomes:UP000220840}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LCDC99A005 {ECO:0000313|EMBL:PEG32823.1,
RC   ECO:0000313|Proteomes:UP000220840};
RA   Bernard K., Burdz T., Wiebe D., Balcewich B., Alfa M., Bernier A.-M.;
RT   "Effective Description of Clostridium neonatale sp. nov. linked to
RT   necrotizing enterocolitis in neonates and a clarification of species
RT   assignable to the genus Clostridium (Prazmowski 1880) emend. Lawson and
RT   Rainey 2016.";
RL   Submitted (OCT-2017) 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:PEG32823.1}.
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DR   EMBL; PDCJ01000001; PEG32823.1; -; Genomic_DNA.
DR   RefSeq; WP_058296955.1; NZ_PDCJ01000001.1.
DR   AlphaFoldDB; A0A2A7MMV3; -.
DR   STRING; 137838.GCA_001458595_03755; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000220840; 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   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   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   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; 7.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 2.
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:PEG32823.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220840};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          18..478
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          450..491
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   963 AA;  109093 MW;  93417BD368B03FE8 CRC64;
     MAKKTDTLIP KDKNIVGVPL EDAMPENYLP YAIEVAKDRA LPDVRDGLKP VHRRILYGAY
     MLKAFPDRPY YKSARIVGDI LGKYHPHGDT SVYEAMVILA QDFSTRKPLI EGHGNWGSID
     GDGAAAMRYT EARLSPIALE MLRDIDKETV EMIPNYSDSE MEPKVLPSRY PNLLVNGAFG
     IAVGLATNIP PHNLTEVTNG VLAYIDNNEI STKELMEYIK GPDLPTGGIL IGEKSLLSAY
     ETGEGKVAYR AKTSIEKLEN GRLGIVITEF PYRRNKAKLL QTISEMTGDK KHSKVLESIT
     DIRDESDRNG IRAVIEFKKS TDETTADKVL KYLFKKTDLQ CNISFNMVAL ANGKPETMGL
     KAIIKYYVEH QKEIVTKRTI KELEAAKKRY HIVEGFIKAI NILDEVIATI RSSKSKKDAS
     DNLISKYGFT EIQAQAILEL MLYRLTGLEI TAFEKEYAQL EQLIKKLEKI LASEKELLKV
     IKKELKEVTD KYGDERRTQI IHDDTVSKID LEELIVIEDV MVTVSNDGFI KRLPLKNYNR
     SNSNPEDIEY REGDSLKYLI SANTKDTLMI FTNKGFMYQT KGINIPEMKW KEKGERLDRI
     IKTLNLEEEK IVSIISLDNL NPDKAFKFMT SRGGIKITSL EKFKTSYTKL QALKLKEYDE
     LISVNLKELK DEEKNLKIKT KLGLEFTLEV PEIEEAGRNI LPVQLFNLSD HDEVINVEEV
     EGIDYFELNI GINEKGKLKA YKTVKEDLLK VKTNSLSELM IFTNIGNVYK IPVFLMKKLM
     EEEVSVETFV GALDKKEKVV TLMSVNSYEE DTVVYLFSKK GMVKKTLLKE FEGDVLKQAC
     YKFKFEDDEV VAADINKIKL GYLVMITKKG MAIRFPVENV NPMGKIASGV TGISLREDDE
     VIFGKFTSDY VEAGGNTIVL TTNSKQKENI NIKDIKLQNR AGRGNNMIVL VLGDEIKNIN
     IDN
//
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