(data stored in SCRATCH3701 zone)

HOGENOM6: CROTZ_1_PE2876

ID   CROTZ_1_PE2876                       STANDARD;      PRT;   878 AA.
AC   CROTZ_1_PE2876; C9XWM9;
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; EC=5.99.1 3; (CROTZ_1.PE2876).
GN   Name=gyrA; OrderedLocusNames=Ctu_28760; ORFNames=CTU_28760;
OS   CRONOBACTER TURICENSIS Z3032.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=693216;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CROTZ_1.PE2876.
CC       Cronobacter turicensis z3032, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:C9XWM9_CROTZ
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; C9XWM9; -.
DR   EMBL; FN543093; CBA32359.1; -; Genomic_DNA.
DR   RefSeq; YP_003211239.1; NC_013282.2.
DR   STRING; C9XWM9; -.
DR   GeneID; 8461513; -.
DR   GenomeReviews; FN543093_GR; Ctu_28760.
DR   KEGG; ctu:Ctu_28760; -.
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; CROTZ_1.PE2876; -.
DR   PRODOM; CROTZ_1_PE2876.
DR   SWISS-2DPAGE; CROTZ_1_PE2876.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   878 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDLAREITP VNIEEELKNS YLDYAMSVIV GRALPDVRDG LKPVHRRVLY AMNVLGNDWN
     KAYKKSARVV GDVIGKYHPH GDSAVYDTIV RMAQPFSLRY TLVDGQGNFG SIDGDSAAAM
     RYTEIRLAKI AHELMADLDK ETVDFVDNYD GTEKIPDVMP TKIPNLLVNG SSGIAVGMAT
     NIPPHNLTEV INGCLAYIDD EDISIEGLME HIPGPDFPTS AIINGRRGIE EAYRTGRGKI
     YIRARAEVEV DPKNGRETII VHEIPYQVNK ARLIEKIAEL VKDKRVEGIS ALRDESDKDG
     MRIVIEIKRD AVGEVVLNNL YSQTQLQVSF GINMVALHHG QPKIMALKEI LAAFVRHRRE
     VVTRRTIFEL RKARERAHIL EGLAIALANI DPIIELIRRA PNPSEAKAGL IAQAWELGTV
     SAMLERAGDD AARPEWLEPE FGIRDGKYWL TEQQAQAILD LRLQKLTGLE HEKLLDEYKE
     LLEQIAELLH ILGSADRLME VIREELELIR DQFGDERRTE ITANSADINI EDLINQEDVV
     VTLSHQGYVK YQPLTDYEAQ RRGGKGKSAA RIKEEDFIDR LLVANTHDTI LCFSSRGRLY
     WMKVYQLPEA SRGARGRPIV NLLPLEANER ITAILPVREY EEGVNVFMAT ASGTVKKTAL
     TEFSRPRTAG IIAVNLNEGD ELIGVDLTAG KDEVMLFSAQ GKVVRFKEDA VRPMGRTATG
     VRGIRLGEGD SVVSLIVPRG EGAILTATQN GYGKRTAVEE YPTKSRATKG VISIKVTDRN
     GPVVGAVQVD DADQIMMITD AGTLVRTRVS EISVVGRNTQ GVILIRTAED ENVVGLQRVA
     EPVDDEELDS IDGSVAEGDD EIAPETDVDD DAADDADE
//

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