(data stored in SCRATCH3701 zone)

HOGENOM6: CAMJM_1_PE962

ID   CAMJM_1_PE962                        STANDARD;      PRT;   863 AA.
AC   CAMJM_1_PE962; E1PPJ6;
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; (CAMJM_1.PE962).
GN   Name=gyrA; OrderedLocusNames=CJM1_1001;
OS   CAMPYLOBACTER JEJUNI SUBSP. JEJUNI M1.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=645464;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CAMJM_1.PE962.
CC       Campylobacter jejuni (subsp. jejuni, serovar HS21, strain M1 / 99/308)
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:E1PPJ6_CAMJM
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; E1PPJ6; -.
DR   EMBL; CP001900; ADN91196.1; -; Genomic_DNA.
DR   ProteinModelPortal; E1PPJ6; -.
DR   SMR; E1PPJ6; 33-488.
DR   GenomeReviews; CP001900_GR; CJM1_1001.
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; CAMJM_1.PE962; -.
DR   PRODOM; CAMJM_1_PE962.
DR   SWISS-2DPAGE; CAMJM_1_PE962.
KW   ADN91196.100008510fold_1320000031;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   863 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MENIFSKDSD IELVDIENSI KSSYLDYSMS VIIGRALPDA RDGLKPVHRR ILYAMQNDEA
     KSRTDFVKSA RIVGAVIGRY HPHGDTAVYD ALVRMAQDFS MRYPSITGQG NFGSIDGDSA
     AAMRYTEAKM SKLSHELLKD IDKDTVDFVP NYDGSESEPD VLPSRVPNLL LNGSSGIAVG
     MATNIPPHSL NELIDGLLYL LDNKDASLEE IMQFIKGPDF PTGGIIYGKK GIIEAYRTGR
     GRVKVRAKTH IEKKTNKDVI VIDELPYQTN KARLIEQIAE LVKERQIEGI SEVRDESNKE
     GIRVVIELKR EAMSEIVLNN LFKSTTMEST FGVIMLAIHN KEPKIFSLLE LLNLFLTHRK
     TVIIRRTIFE LQKARARAHI LEGLKIALDN IDEVIALIKN SSDNNTARDS LVAKFGLSEL
     QANAILDMKL GRLTGLEREK IENELAELMK EIARLEEILK SETLLENLIR DELKEIRSKF
     DVPRITQIED DYDDIDIEDL IPNENMVVTI THRGYIKRVP SKQYEKQKRG GKGKLAVTTY
     DDDFIESFFT ANTHDTLMFV TDRGQLYWLK VYKIPEGSRT AKGKAVVNLI NLQAEEKIMA
     IIPTTDFDES KSLCFFTKNG IVKRTNLSEY QNIRSVGVRA INLDENDELV TAIIVQRDED
     EIFASGGEEN LENQEIENLD DENLENEESV STQGKMLFAV TKKGMCIKFP LAKVREIGRV
     SRGVTAIKFK EKNDELVGAV VIENDEQEIL SISAKGIGKR TNAGEYRLQS RGGKGVICMK
     LTEKTKDLIS VVIVDETMDL MALTSSGKMI RVDMQSIRKA GRNTSGVIVV NVENDEVVSI
     AKCPKEENDE DELSDENFGL DLQ
//

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