AMIC_ECOL6
ID AMIC_ECOL6 Reviewed; 417 AA.
AC P63884; Q46929;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase AmiC;
DE EC=3.5.1.28;
DE Flags: Precursor;
GN Name=amiC; OrderedLocusNames=c3411;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell
CC division. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN81856.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN81856.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000016907.1; NC_004431.1.
DR AlphaFoldDB; P63884; -.
DR SMR; P63884; -.
DR STRING; 199310.c3411; -.
DR EnsemblBacteria; AAN81856; AAN81856; c3411.
DR GeneID; 66673316; -.
DR KEGG; ecc:c3411; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_2_6; -.
DR OMA; KRYFAAN; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Hydrolase; Periplasm; Signal.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 32..417
FT /note="N-acetylmuramoyl-L-alanine amidase AmiC"
FT /id="PRO_0000006466"
FT DOMAIN 190..404
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000255"
FT REGION 166..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 417 AA; 45634 MW; 76F8F733DCCC36D7 CRC64;
MSGSNTAISR RRLLQGAGAM WLLSVSQVSL AAVSQVVAVR VWPASSYTRV TVESNRQLKY
KQFALSNPER VVVDIEDVNL NSVLKGMAAQ IRADDPFIKS ARVGQFDPQT VRMVFELKQN
VKPQLFALAP VAGFKERLVM DLYPANAQDM QDPLLALLED YNKGDLEKQV PPAQSGPQPG
KAGRDRPIVI MLDPGHGGED SGAVGKYKTR EKDVVLQIAR RLRSLIEKEG NMKVYMTRNE
DIFIPLQVRV AKAQKQRADL FVSIHADAFT SRQPSGSSVF ALSTKGATST AAKYLAQTQN
ASDLIGGVSK SGDRYVDHTM FDMVQSLTIA DSLKFGKAVL NKLGKINKLH KNQVEQAGFA
VLKAPDIPSI LVETAFISNV EEERKLKTAT FQQEVAESIL AGIKAYFADG ATLARRG
