ID B1L243_CLOBM Unreviewed; 398 AA.
AC B1L243;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=N(4)-bis(aminopropyl)spermidine synthase C-terminal domain-containing protein {ECO:0000259|Pfam:PF01861};
GN OrderedLocusNames=CLK_2780 {ECO:0000313|EMBL:ACA55320.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA55320.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA55320.1, ECO:0000313|Proteomes:UP000000722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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DR EMBL; CP000962; ACA55320.1; -; Genomic_DNA.
DR RefSeq; WP_012343318.1; NC_010520.1.
DR AlphaFoldDB; B1L243; -.
DR KEGG; cbl:CLK_2780; -.
DR HOGENOM; CLU_042160_0_0_9; -.
DR Proteomes; UP000000722; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0034641; P:cellular nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002723; BpsA_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR23290:SF0; RRNA N6-ADENOSINE-METHYLTRANSFERASE METTL5; 1.
DR PANTHER; PTHR23290; UNCHARACTERIZED; 1.
DR Pfam; PF01861; BpsA_C; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
FT DOMAIN 114..308
FT /note="N(4)-bis(aminopropyl)spermidine synthase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01861"
SQ SEQUENCE 398 AA; 45267 MW; CD3E5C4EF88ABF36 CRC64;
MRNNYVDIIY QNVKIQEGRQ AIEKLLIDFY FACGYSSKDY AILNNIPVPL VTAIKNEALK
LKLLEKSTGI HLSLKGKQFV KNELGYKGIN IELYKTLNIN NVGKVMERLS LNLNNIFENR
PEADVSIDQS KCTLETAIKR ALLCLENNCL IGKNILCVGD DDLISVSTGM LLHTLYGGNM
NLCKTKIYVL DSDQRILDYI CEVAKLYDLP INCYNIDFRD SIPNEYISKM DCFYTDPPYT
LSGMKLFLSR GLECLKNSVS LNVFLSYAHK SQEEMLKIHK IFIELGLSAL RIMPKFNRYE
GAGILGNSSQ MLLLKTTSAA RSPIIGEKFN IPIYTGEIKK TRRKYSCKNC NTTHYVSLED
TYSTIEKLKT AGCTICGHHF FNMVSKKEIL NVDKKSYK
//
