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Database: UniProt
Entry: S5LVU9_9MOLU
LinkDB: S5LVU9_9MOLU
Original site: S5LVU9_9MOLU 
ID   S5LVU9_9MOLU            Unreviewed;       811 AA.
AC   S5LVU9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
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:AGR40701.1};
GN   ORFNames=STAIW_v1c00040 {ECO:0000313|EMBL:AGR40701.1};
OS   Spiroplasma taiwanense CT-1.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=1276220 {ECO:0000313|EMBL:AGR40701.1, ECO:0000313|Proteomes:UP000014984};
RN   [1] {ECO:0000313|EMBL:AGR40701.1, ECO:0000313|Proteomes:UP000014984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CT-1 {ECO:0000313|EMBL:AGR40701.1};
RX   PubMed=23873917; DOI=10.1093/gbe/evt108;
RA   Lo W.S., Ku C., Chen L.L., Chang T.H., Kuo C.H.;
RT   "Comparison of metabolic capacities and inference of gene content evolution
RT   in mosquito-associated Spiroplasma diminutum and S. taiwanense.";
RL   Genome Biol. Evol. 5:1512-1523(2013).
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}.
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DR   EMBL; CP005074; AGR40701.1; -; Genomic_DNA.
DR   RefSeq; WP_020833840.1; NC_021846.1.
DR   AlphaFoldDB; S5LVU9; -.
DR   STRING; 1276220.STAIW_v1c00040; -.
DR   KEGG; stai:STAIW_v1c00040; -.
DR   PATRIC; fig|1276220.3.peg.4; -.
DR   eggNOG; COG0188; Bacteria.
DR   HOGENOM; CLU_002977_6_1_14; -.
DR   OrthoDB; 9806486at2; -.
DR   Proteomes; UP000014984; Chromosome.
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   NCBIfam; TIGR01063; gyrA; 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; 6.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014984};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          13..465
FT                   /note="DNA topoisomerase type IIA"
FT                   /evidence="ECO:0000259|SMART:SM00434"
FT   COILED          437..464
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   811 AA;  92419 MW;  7227AC35416786A0 CRC64;
     MSEVFNKGRI LEIDIKNEVE KDFLEYSMSV IVSRALPDLR DGLKPVHRRI IYAMNDLKIT
     ADTPHKKSAR IVGEVIGKYH PHGDSSVYEA MVRMSQDFSY RYPLVEGHGN FGSIDGDGAA
     AMRYTEARLS KISSMLLKDI DMNTVPYIDN YDASEQEPKY LTGYFPNLLV NGATGIAVGM
     ATSIPPHNLI EVINATIEYI KNNNITIEEI LKFIKGPDFP TGALMTNGKN MIEGYKTGKG
     NLTIRAKIDI EETNKNQKII ISEIPYQTNK LKIVEKIAEL YKNKIITGIS DIRDESNYEG
     IRIVLEFSKN SNPQLIIKRL YKFTNLQSNF TINMLSLHNG IPVVLNIKEI IKFYVKFQIE
     IILKRSIFEK EKLEAKLHIL NAIRTAVDHI DEIIKIIKNS NTTEIAYKKL FDNFNFDEKQ
     SKAILDMRLQ RLVGLEREKI ENDINNIELR IKELIKILES KEEQNILLID QLEYIKNKFG
     DERRTKIIEE DDIQIDDEEL IQDTQMILTL SEEGYIRRLQ PEEFKTQKRG GKGIIINSNL
     DDNILIAKMG KTKDDVLFFS NEGKVYKLKG YNITQFLRTS RGVPIINFIG INFSEKVSSV
     LTFRNKKNNY KYLVFVTKKG IVKKVNLEEF NKINNFGKIA IHLDKEDSLI SVIPTSGLDK
     ILIATKNGKV SKINESDFRP MSRSSRGVKG ITLDKTDEVI SSCTDFKNDC VVTISEKGII
     KKTLISEYNN FNRGAKGVVG MKLNDKTGKL KSVLAIRETD EVLMISSKGK IIKIHSQEIK
     MQSRNTSGVI GFNLEDDEKI TAVTLEWNKG D
//
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