(data stored in SCRATCH3701 zone)

HOGENOM6: LISM2_1_PE2960

ID   LISM2_1_PE2960                       STANDARD;      PRT;   842 AA.
AC   LISM2_1_PE2960; D2PBI4;
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 subunit A; (LISM2_1.PE2960).
GN   Name=gyrA; OrderedLocusNames=LM5923_2965;
OS   LISTERIA MONOCYTOGENES 08-5923.
OC   Bacteria; Firmicutes; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=637381;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS LISM2_1.PE2960.
CC       Listeria monocytogenes 08-5923, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:D2PBI4_LISM2
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; D2PBI4; -.
DR   EMBL; CP001604; ADB72806.1; -; Genomic_DNA.
DR   RefSeq; YP_003418168.1; NC_013768.1.
DR   ProteinModelPortal; D2PBI4; -.
DR   SMR; D2PBI4; 31-487.
DR   GeneID; 8759759; -.
DR   GenomeReviews; CP001604_GR; LM5923_2965.
DR   KEGG; lmy:LM5923_2965; -.
DR   OMA; TGRGRIY; -.
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:InterPro.
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; LISM2_1.PE2960; -.
DR   PRODOM; LISM2_1_PE2960.
DR   SWISS-2DPAGE; LISM2_1_PE2960.
KW   DNA gyrase subunit A;
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 DPEITIRDLM 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 SYLFFTTKHG VVKRTTLSQF AKIRQSGLRA VELRENDELI SVQMTDGSKN
     MIIATKHGQS IYFPEENIRV MGRTAAGVRG IRLREDDEVI GMEVLEDDEK VLVVTEKGYG
     KQTPASQYPL RNRGGMGVKT VTITEKNGNL VAMKTVTGEE DLMLMTVSGV LIRFEIDTVS
     QTGRSAMGVK LIRLDEDEKV ATVAKVPKEE DEVELEEEID ETLITQVPDE SFEDAPGSDI
     EE
//

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