ID   MCJC_ECOLX              Reviewed;         513 AA.
AC   Q9X2V9; Q333M5;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Microcin J25-processing protein McjC;
GN   Name=mcjC;
OS   Escherichia coli.
OG   Plasmid pTUC100, and Plasmid pTUC202.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=AY25; PLASMID=pTUC100;
RX   PubMed=10198038; DOI=10.1128/jb.181.8.2659-2662.1999;
RA   Solbiati J.O., Ciaccio M., Farias R.N., Gonzalez-Pastor J.E., Moreno F.,
RA   Salomon R.A.;
RT   "Sequence analysis of the four plasmid genes required to produce the
RT   circular peptide antibiotic microcin J25.";
RL   J. Bacteriol. 181:2659-2662(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=AY25; PLASMID=pTUC202;
RX   PubMed=17656316; DOI=10.1016/j.chembiol.2007.06.004;
RA   Duquesne S., Destoumieux-Garzon D., Zirah S., Goulard C., Peduzzi J.,
RA   Rebuffat S.;
RT   "Two enzymes catalyze the maturation of a lasso peptide in Escherichia
RT   coli.";
RL   Chem. Biol. 14:793-803(2007).
CC   -!- FUNCTION: Along with McjB, necessary and sufficient to process the
CC       inactive microcin J25 (McjA) precursor into the active peptide. May be
CC       involved in the formation of the amide bond between Gly-38 and Glu-53
CC       of McjA. {ECO:0000269|PubMed:10198038, ECO:0000269|PubMed:17656316}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD28496.1; Type=Miscellaneous discrepancy; Note=Has 3 extra noncontiguous nucleotides compared to the shown sequence. Removing these nucleotides suprresses the original stop codon at position 443.; Evidence={ECO:0000305};
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DR   EMBL; AF061787; AAD28496.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AM116873; CAJ40934.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9X2V9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00733; Asn_synthase; 1.
PE   4: Predicted;
KW   Antibiotic biosynthesis; Cytoplasm; Plasmid.
FT   CHAIN           1..513
FT                   /note="Microcin J25-processing protein McjC"
FT                   /id="PRO_0000068577"
FT   DOMAIN          176..436
FT                   /note="Asparagine synthetase"
SQ   SEQUENCE   513 AA;  58710 MW;  7D1D201EFE250D31 CRC64;
     MEIFNVKLND TSIRIIFCKT LSAFRTENTI VMLKGKAVSN GKPVSTEEIA RVVEEKGVSE
     VIENLDGVFC ILIYHFNDLL IGKSIQSGPA LFYCKKNMDI FVSDKISDIK FLNPDMTFSL
     NITMAEHYLS GNRIATQESL ITGIYKVNNG EFIKFNNQLK PVLLRDEFSI TKKNNSTIDS
     IIDNIEMMRD NRKIALLFSG GLDSALIFHT LKESGNKFCA YHFFSDESDD SEKYFAKEYC
     SKYGVDFISV NKNINFNEKL YFNLNPNSPD EIPLIFEQTD EEGEGQPPID DDLLYLCGHG
     GDHIFGQNPS ELFGIDAYRS HGLMFMHKKI VEFSNLKGKR YKDIIFSNIS AFINTSNGCS
     PAKQEHVSDM KLASAQFFAT DYTGKINKLT PFLHKNIIQH YAGLPVFSLF NQHFDRYPVR
     YEAFQRFGSD IFWKKTKRSS SQLIFRILSG KKDELVNTIK QSGLIEILGI NHIELESILY
     ENTTTRLTME LPYILNLYRL AKFIQLQSID YKG