AMI_LISMG
ID AMI_LISMG Reviewed; 917 AA.
AC O33983;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Protein Ami {ECO:0000303|PubMed:9282740};
DE EC=3.2.1.- {ECO:0000305|PubMed:9282740};
DE AltName: Full=Autolysin {ECO:0000305|PubMed:9282740};
DE Flags: Precursor;
GN Name=ami {ECO:0000303|PubMed:9282740};
OS Listeria monocytogenes serotype 1/2a (strain EGD / Mackaness).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1334565;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, DOMAIN,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=EGD / Mackaness;
RX PubMed=9282740; DOI=10.1046/j.1365-2958.1997.4621825.x;
RA Braun L., Dramsi S., Dehoux P., Bierne H., Lindahl G., Cossart P.;
RT "InlB: an invasion protein of Listeria monocytogenes with a novel type of
RT surface association.";
RL Mol. Microbiol. 25:285-294(1997).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=EGD / Mackaness;
RX PubMed=10594817; DOI=10.1046/j.1365-2958.1999.01652.x;
RA Jonquieres R., Bierne H., Fiedler F., Gounon P., Cossart P.;
RT "Interaction between the protein InlB of Listeria monocytogenes and
RT lipoteichoic acid: a novel mechanism of protein association at the surface
RT of Gram-positive bacteria.";
RL Mol. Microbiol. 34:902-914(1999).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=EGD / Mackaness;
RX PubMed=10746777; DOI=10.1099/00221287-146-3-731;
RA Milohanic E., Pron B., Berche P., Gaillard J.-L.;
RT "Identification of new loci involved in adhesion of Listeria monocytogenes
RT to eukaryotic cells.";
RL Microbiology 146:731-739(2000).
CC -!- FUNCTION: A bacteriolysin able to lyse both L.monocytogenes and
CC S.aureus. {ECO:0000305|PubMed:9282740}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:9282740}. Cell
CC membrane {ECO:0000305|PubMed:10594817}. Note=Anchored by its GW repeats
CC to the cell surface. {ECO:0000305|PubMed:9282740}.
CC -!- DOMAIN: The C-terminus has 8 GW repeats. {ECO:0000305|PubMed:9282740}.
CC -!- DISRUPTION PHENOTYPE: Decrease in lytic activity on L.monocytogenes and
CC S.aureus (PubMed:9282740). Decreased adhesion to mammalian host cells,
CC however no change in host invasion and host intracellular growth
CC (PubMed:10746777). {ECO:0000269|PubMed:10746777,
CC ECO:0000269|PubMed:9282740}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the N-acetylmuramoyl-
CC L-alanine amidase 2 family. {ECO:0000305}.
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DR EMBL; U82488; AAC45605.1; -; Genomic_DNA.
DR AlphaFoldDB; O33983; -.
DR SMR; O33983; -.
DR MoonProt; O33983; -.
DR GO; GO:0009986; C:cell surface; IDA:CAFA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0044651; P:adhesion of symbiont to host epithelial cell; IDA:CAFA.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IMP:CAFA.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 2.30.30.170; -; 8.
DR Gene3D; 3.40.80.10; -; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR025987; GW_dom.
DR InterPro; IPR038200; GW_dom_sf.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF13457; GW; 8.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
DR PROSITE; PS51780; GW; 8.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Repeat; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..917
FT /note="Protein Ami"
FT /evidence="ECO:0000255"
FT /id="PRO_5004158194"
FT DOMAIN 118..245
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT DOMAIN 279..358
FT /note="GW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 361..435
FT /note="GW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 440..519
FT /note="GW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 522..596
FT /note="GW 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 601..679
FT /note="GW 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 682..756
FT /note="GW 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 761..840
FT /note="GW 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT DOMAIN 843..917
FT /note="GW 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01116"
FT REGION 262..917
FT /note="GW repeat region, necessary and sufficient for cell
FT surface attachment"
FT /evidence="ECO:0000269|PubMed:9282740"
SQ SEQUENCE 917 AA; 102353 MW; 21EA2452B4F103B7 CRC64;
MKKLVKSAVV FAGLVFIGTS ATMITEKASA ASTDPVQKVD GQATYIPKGV RDGTATEEHD
GFEDGTNSVL QQVPLLRATT GYPDVNAYIK SNKFSTAKIE KQLKSQFPKF NYRNGYGKPE
GIVIHETANN SSTITGEINY MSTNYNNAFV HAFVDKSRII QIHPTENGVW GAGQYANARF
IQVELVRSKT FDEFARSINN YAYYAAYLLD QYNLPVDSAH SDGKGTVWSH DAVTRYLGGT
THTDPVAYFN QWGYNFNNFV SLINEKYKAM QVNYEKIEYD KAITAYSRVK TATGNSVWTK
PNKTEGAKLV NPLSSYSGKN LRIIREAKTS GGTIWYQFSV GGKTIGWVDS KALNTFYTPS
MEKTITGTRY VLPSKQTVHY YGLPVEDSAI DRGPLSKFNG QALTLQREAT IEGQLWYRVK
DLGWVKAVNL TTTKYDLIEY DKAITAYSRV KTAAGNYVWS KPNKTEGAKQ GSALSTYSGK
NMRIIREAKT SSGTIWYQFS IDGKTIGWVD TKALNTFYTP SMEKNLTATR YVAPGQETQH
YYGLPVADSA IDRGPLSKFA GQTLTVQREA TIEGQLWYRV KDLGWTKAST LTATQYDKLE
YDKAITAYSR VKTATGNSVW TKPYRTSGYK LVNPLSSYAG KNLRIIREAK TSSGIWYQFS
VGGKTIGWVD SKALNTFYTP SMEKTITGTR YVLPSKQTVH YYGLPVEDSA IDRGPLSKFN
GQALTLQREA TIEGQLWYRV KDLGWVKAAN LTTTKYDTLS YDKAITAYSR VKTATGNSVW
TKPNKIEGAQ KISALSTYSG KNMRILREAK TSSGTIWYQF SVGGKTIGWV ETKALNTFYT
PSMEKNLTAT RYVLTSKKNE HYYGLPVVDS AIDRGPLSKF SGKTLTVQRE ATIEGQLWYR
VKDLGWTKAA NLSAKKQ
