LOCUS NP_978569 236 aa linear BCT 20-JUL-2008
DEFINITION ABC transporter, ATP-binding protein [Bacillus cereus ATCC 10987].
ACCESSION NP_978569
VERSION NP_978569.1 GI:42781322
DBSOURCE REFSEQ: accession NC_003909.8
KEYWORDS .
SOURCE Bacillus cereus ATCC 10987
ORGANISM Bacillus cereus ATCC 10987
Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus; Bacillus
cereus group.
REFERENCE 1 (residues 1 to 236)
AUTHORS Rasko,D.A., Ravel,J., Okstad,O.A., Helgason,E., Cer,R.Z., Jiang,L.,
Shores,K.A., Fouts,D.E., Tourasse,N.J., Angiuoli,S.V., Kolonay,J.,
Nelson,W.C., Kolsto,A.-B., Fraser,C.M. and Read,T.D.
TITLE The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
adaptations and a large plasmid related to Bacillus anthracis pXO1
JOURNAL Nucleic Acids Res. 32 (3), 977-988 (2004)
PUBMED 14960714
REFERENCE 2 (residues 1 to 236)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (10-SEP-2004) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 236)
AUTHORS Rasko,D.A., Ravel,J., Okstad,O.A., Helgason,E., Cer,R.Z., Jiang,L.,
Shores,K.A., Fouts,D.E., Tourasse,N.J., Angiuoli,S.V., Kolonay,J.,
Nelson,W.C., Kolsto,A.-B., Fraser,C.M. and Read,T.D.
TITLE Direct Submission
JOURNAL Submitted (19-FEB-2004) The Institute for Genomic Research, 9712
Medical Center Dr, Rockville, MD 20850, USA
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from AAS41177.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..236
/organism="Bacillus cereus ATCC 10987"
/strain="ATCC 10987"
/db_xref="ATCC:10987"
/db_xref="taxon:222523"
Protein 1..236
/product="ABC transporter, ATP-binding protein"
/calculated_mol_wt=26660
Region 1..236
/region_name="FepC"
/note="ABC-type cobalamin/Fe3+-siderophores transport
systems, ATPase components [Inorganic ion transport and
metabolism / Coenzyme metabolism]; COG1120"
/db_xref="CDD:31317"
Region 18..202
/region_name="ABC_DR_subfamily_A"
/note="This family of ATP-binding proteins belongs to a
multisubunit transporter involved in drug resistance (BcrA
and DrrA), nodulation, lipid transport, and lantibiotic
immunity. In bacteria and archaea, these transporters
usually include an ATP-binding...; cd03230"
/db_xref="CDD:72989"
Site 35..42
/site_type="other"
/note="Walker A/P-loop"
/db_xref="CDD:72989"
Site order(38..39,41..43,73,149..150,182)
/site_type="other"
/note="ATP binding site"
/db_xref="CDD:72989"
Site 70..73
/site_type="other"
/note="Q-loop/lid"
/db_xref="CDD:72989"
Site order(89,126..134)
/site_type="other"
/note="ABC transporter signature motif"
/db_xref="CDD:72989"
Site 145..150
/site_type="other"
/note="Walker B"
/db_xref="CDD:72989"
Site 153..156
/site_type="other"
/note="D-loop"
/db_xref="CDD:72989"
Site 178..184
/site_type="other"
/note="H-loop/switch region"
/db_xref="CDD:72989"
CDS 1..236
/locus_tag="BCE_2258"
/coded_by="NC_003909.8:2163981..2164691"
/note="identified by match to protein family HMM PF00005"
/transl_table=11
/db_xref="GeneID:2751628"
ORIGIN
1 mlevnirsag yeigektihd iafsieqgel valigangag ksttiktmlg llvnvdgeis
61 fgekknpyay vpehptyydy ltlwehiell maareneags werkaeellh mfrmdkhkhe
121 ylskfskgmk qksmlilafl tepdfyiide pfigldpvat keflsylyke kergagillc
181 thvldtaeri cerfllisqg tlvadghlea iqtlaempgs slldcfdviv rreqhd
//