(data stored in SCRATCH3701 zone)

HOGENOM6: LISMH_1_PE2625

ID   LISMH_1_PE2625                       STANDARD;      PRT;   842 AA.
AC   LISMH_1_PE2625; B8DAQ3;
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; (LISMH_1.PE2625).
GN   Name=gyrA; OrderedLocusNames=LMHCC_2657;
OS   LISTERIA MONOCYTOGENES HCC23.
OC   Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LISMH_1.PE2625.
CC       Listeria monocytogenes HCC23, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:B8DAQ3_LISMH
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; B8DAQ3; -.
DR   EMBL; CP001175; ACK40992.1; -; Genomic_DNA.
DR   RefSeq; YP_002351606.1; NC_011660.1.
DR   STRING; B8DAQ3; -.
DR   GeneID; 7080931; -.
DR   GenomeReviews; CP001175_GR; LMHCC_2657.
DR   KEGG; lmh:LMHCC_2657; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
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; LISMH_1.PE2625; -.
DR   PRODOM; LISMH_1_PE2625.
DR   SWISS-2DPAGE; LISMH_1_PE2625.
KW   DNA gyrase, A subunit;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   842 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAETPNQRIT EINLNKEMRT SFLDYAMSVI VARALPDVRD GLKPVHRRIL YAMNDLGMTS
     DKAYKKSARI VGEVIGKYHP HGDTAVYFTM VRMAQDFSYR NMLVDGHGNF GSVDGDMAAA
     MRYTEARMSK ISMELLRDIN KDTIDYADNY DGSEREPVIL PARFPNLLVN GSSGIAVGMA
     TNIPTHHLGE VIDGVLALSH NPEITIRDLM EYIPGPDFPT AGMIMGRSGI RRAYESGRGS
     ITVRGRVDIE EKKNGKETIV ITEIPYQVNK ARLVERIAEL AREKKIDGIT SLNDESDRSG
     MRIVIEVRRD ISASVIVNNL FKMTALQTTF GINMLALVDN HPKVLNLKEI LYHYLEHQKV
     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 SYLFFTTKHG VVKRTTLSQF AKIRQSGLRA VELRENDELI SVQMTDGSKN
     MIIATKHGQS IYFPEENIRV MGRTAAGVRG IRLREDDEVI GMEVLEDDEK VLVVTEKGYG
     KQTPASQYPL RNRGGMGVKT VTITEKNGNL VAMKTVTGEE DLMLMTVSGV LIRFEIETVS
     QTGRSAMGVK LIRLDEDEKV ATVAKVPKEE DEVELEEEID ETLITQVPDE SFEDAPGSDI
     EE
//

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