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Database: UniProt
Entry: W0ZAH6_9MICO
LinkDB: W0ZAH6_9MICO
Original site: W0ZAH6_9MICO 
ID   W0ZAH6_9MICO            Unreviewed;       809 AA.
AC   W0ZAH6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN   Name=gyrA {ECO:0000313|EMBL:CDK00738.1};
GN   ORFNames=MIC448_320042 {ECO:0000313|EMBL:CDK00738.1};
OS   Microbacterium sp. C448.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1177594 {ECO:0000313|EMBL:CDK00738.1, ECO:0000313|Proteomes:UP000028883};
RN   [1] {ECO:0000313|EMBL:CDK00738.1, ECO:0000313|Proteomes:UP000028883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C448 {ECO:0000313|EMBL:CDK00738.1,
RC   ECO:0000313|Proteomes:UP000028883};
RX   PubMed=24526651; DOI=10.1128/genomeA.01113-13;
RA   Martin-Laurent F., Marti R., Waglechner N., Wright G.D., Topp E.;
RT   "Draft Genome Sequence of the Sulfonamide Antibiotic-Degrading
RT   Microbacterium sp. Strain C448.";
RL   Genome Announc. Announc.2:e01113-e01113(2014).
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:CDK00738.1}.
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DR   EMBL; CBVQ010000195; CDK00738.1; -; Genomic_DNA.
DR   RefSeq; WP_036295772.1; NZ_HG779612.1.
DR   AlphaFoldDB; W0ZAH6; -.
DR   STRING; 1177594.MIC448_320042; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_11; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000028883; 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; 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; 2.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:CDK00738.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028883};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          16..469
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   REGION          775..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   809 AA;  86820 MW;  59D9BE11443B28E5 CRC64;
     MPAPVSEPPA ERIEDVDVSS EMQGSFLEYA YSVIYSRALP DARDGMKPVQ RRIVYQMSEM
     GLRPDRGHVK SARVVGEVMG KLHPHGDAPI YDALVRLAQP FSQRVPMVDG HGNFGSLDDG
     PAASRYTEAR LAPAALAMAE GLDEDVVDFI PNYDNQFQQP EVLPAAYPNL LVNGASGIAV
     GMATNMAPHN LIEVVGAAIH LLENPDATLD DLMAYVPGPD LPSGGVIVGL EGVRDAYETG
     RGSFKTRAKT SIESLGPRKT GIVVTELPYL VGPERVIEKI KDAVQSKKLQ GISDVADLTD
     RTHGTRLVIG IKTGFDPQAV LDQLYRLTPL EDSFSINNVA LVEGQPRTLG LRELLRVYVD
     HRLSVVTRRS RYRLDRRRER LHLVDGLLIA ILDIDEVIQV IRASDDGEQA RTRLMEVFDL
     SQLQAEYILE LRLRRLTKFS RIELEAERDQ LLAEIAQLEE LLGSDALLRK QVATELDAIA
     EKLGTPRRTL LTNAAPAVAR PSRNAPILEI VDAPTIVVLS TTGRAVRVDL SEGTEIVSPT
     RRSKHDALLT DVRTTVRGEL GAITNRGRML RFSPVDLPSV PPASVQLAAG VALRDYLGLT
     DKAERVVMLT RLDIDTPLAI GTRQGVVKRI IPSALPPKPE IEIIALKPGD GVVGAASAPD
     ESELVFVSDD ARLLRFAASS VRPQGASAGG MAGMNIGSAN AIFFGSVGEP EAVVVTVSGT
     AGALPGTDAG RAKVSEFAEF PAKGRATGGV RAHAFLKGED ELTLAWVGAT PLRAVGTDGS
     ARTLPEPGAK RDASGQPLDA PVGSVGRAL
//
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