(data stored in SCRATCH3701 zone)

HOGENOM6: LISSS_1_PE7

ID   LISSS_1_PE7                          STANDARD;      PRT;   841 AA.
AC   LISSS_1_PE7; D3UKA0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=DNA gyrase, A subunit; EC=5.99.1 3; (LISSS_1.PE7).
GN   Name=gyrA; OrderedLocusNames=lse_0007;
OS   LISTERIA SEELIGERI SEROVAR 1/2B STR. SLCC3954.
OC   Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=683837;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LISSS_1.PE7.
CC       Listeria seeligeri serovar 1/2b str. SLCC3954, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D3UKA0_LISSS
CC   -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC       stranded DNA in an ATP-dependent manner and also catalyzes the
CC       interconversion of other topological isomers of double-stranded
CC       DNA rings, including catenanes and knotted rings (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA.
CC   -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA
CC       breakage and rejoining; the B chain catalyzes ATP hydrolysis. The
CC       enzyme forms an A2B2 tetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D3UKA0; -.
DR   EMBL; FN557490; CBH26158.1; -; Genomic_DNA.
DR   RefSeq; YP_003463252.1; NC_013891.1.
DR   GeneID; 9082022; -.
DR   GenomeReviews; FN557490_GR; lse_0007.
DR   KEGG; lsg:lse_0007; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   InterPro; IPR020899; Arg_repress_C.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_pinwhl.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a.
DR   InterPro; IPR013760; Topo_IIA_cen.
DR   Gene3D; G3DSA:3.30.1360.40; Arg_repress; 1.
DR   Gene3D; G3DSA:3.90.199.10; Topo_IIA_A/C_ab; 1.
DR   Gene3D; G3DSA:1.10.268.10; Topo_IIA_A_a; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR   TIGRFAMs; TIGR01063; GyrA; 1.
DR   HOGENOMDNA; LISSS_1.PE7; -.
DR   PRODOM; LISSS_1_PE7.
DR   SWISS-2DPAGE; LISSS_1_PE7.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   841 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAETPNQRIT EINLNKEMRT SFLDYAMSVI VARALPDVRD GLKPVHRRIL YAMNDLGMTS
     DKAYKKSARI VGEVIGKYHP HGDTAVYFTM VRMAQDFSYR NMLVDGHGNF GSVDGDMAAA
     MRYTEARMSK ISMELLRDIN KDTIDYADNY DGSEREPVIL PARFPNLLVN GSSGIAVGMA
     TNIPTHHLGE VIDGVLALSN DPDISIRELM EYIPGPDFPT AGMIMGRSGI RRAYESGRGS
     ITVRGRVDIE EKKNGKETIV ITEIPYQVNK ARLVERIAEL AREKKIDGIT SLNDESDRSG
     MRIVIEVRRD ISASVIVNNL FKMTALQTTF GINMLALVDN HPKVLNLKEI LYYYLEHQKV
     VIRRRTEFEL RKAEARAHIL EGLRIALDNI DAIIKLIRGS KTSDVAKEGL MTQFNLSDKQ
     AQAILDMRLQ RLTGLEREKI EEEYQNLVAL INDLKAILAD DERILEIIRE ELEEIKVKYA
     DKRRTEILAG DLVSLEDEDL IPEEEVAITL TKRGYIKRLP LSTYRSQRRG GRGIQGMSTH
     EDDFVEHLVA TSTHDTLLFF TNTGKVYRSK GYEVPEYGRT AKGIPIINLL GIESQEQVNA
     VINLSEFTDD NYLFFTTKHG VVKRTTLSQF AKIRQSGLRA VELRENDELI SVQMTDGNKN
     MIIATKHGQS IYFPEANIRV MGRTAAGVRG IRLREGDEVI GMEVLEDDEK VLVVTEKGYG
     KQTPASQYPL RNRGGMGVKT VTITEKNGNL VAMKTVTGEE DLMLMTVSGV LIRFEIDTVS
     QTGRSAMGVK LIRLDEDEKV ATVAKVPKEE DIELEEEIDE TLITQVPDES FEDAPGSDIE
     E
//

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