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Database: UniProt
Entry: A1XCE7_LEUCI
LinkDB: A1XCE7_LEUCI
Original site: A1XCE7_LEUCI 
ID   A1XCE7_LEUCI            Unreviewed;       393 AA.
AC   A1XCE7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
DE   Flags: Fragment;
GN   Name=gyrB {ECO:0000313|EMBL:ABC87019.1};
OS   Leuconostoc citreum.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=33964 {ECO:0000313|EMBL:ABC87019.1};
RN   [1] {ECO:0000313|EMBL:ABC87019.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CECT4018 {ECO:0000313|EMBL:ABC87019.1};
RA   Chelo I.M., Ze-Ze L., Tenreiro R.;
RT   "Congruence of evolutionary relationships inside the Leuconostoc-
RT   Oenococcus-Weissella clade assessed by phylogenetic analysis of the 16S
RT   rRNA gene, dnaA, gyrB, rpoC and dnaK.";
RL   Int. J. Syst. Evol. Microbiol. 57:276-286(2007).
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 GyrB family.
CC       {ECO:0000256|ARBA:ARBA00010708}.
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DR   EMBL; DQ335683; ABC87019.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1XCE7; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00822; TopoII_Trans_DNA_gyrase; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR000565; Topo_IIA_B.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   PANTHER; PTHR45866:SF1; DNA GYRASE SUBUNIT B, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR45866; DNA GYRASE/TOPOISOMERASE SUBUNIT B; 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   PRINTS; PR01159; DNAGYRASEB.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00433; TOP2c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT   DOMAIN          317..393
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABC87019.1"
FT   NON_TER         393
FT                   /evidence="ECO:0000313|EMBL:ABC87019.1"
SQ   SEQUENCE   393 AA;  43429 MW;  B9E115FF47BF15C9 CRC64;
     GGGYKVSGGL HGVGASVVNA LSTNLDVKVV RDGQVYYMDF KVGRVNTRMV KLDEKPTIAR
     GTIVHFKPDA DIFRETTTFN YNTLLTRVRE LAFLNKGLRI SITDNRAETP MTESFHYEGG
     IKEYVKYLNA EKVVVFPEPV YVEGEENGIV VEAALQYTTD VKDSLRTFTN NINTYEGGTH
     ETGFKTALTR VINDYARKNG QLKENAESLT GEDVREGMTA IVSIKHPDPQ FEGQTKTKLG
     NSDARQATDR MFSETFSRFM MENPAVAKQI VEKGILAQKA RLAAKRAREM TRKQSGLEIG
     NLPGKLADNT SNDPAISELF IVEGDSAGGS AKQGRNRLTQ AILPIRGKIL NVEKATLDKV
     LANEEIRSLF TAMGTGFGDD FNVEKANYHK VII
//
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