AMIA_ECOLI
ID AMIA_ECOLI Reviewed; 289 AA.
AC P36548; P78199;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase AmiA;
DE EC=3.5.1.28;
DE Flags: Precursor;
GN Name=amiA; Synonyms=yfeE; OrderedLocusNames=b2435, JW2428;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8300522; DOI=10.1128/jb.176.3.673-680.1994;
RA Troup B., Jahn M., Hungerer C., Jahn D.;
RT "Isolation of the hemF operon containing the gene for the Escherichia coli
RT aerobic coproporphyrinogen III oxidase by in vivo complementation of a
RT yeast HEM13 mutant.";
RL J. Bacteriol. 176:673-680(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RX PubMed=1903834; DOI=10.1007/bf00260648;
RA Tanaka K., Muramatsu S., Yamada H., Mizuno T.;
RT "Systematic characterization of curved DNA segments randomly cloned from
RT Escherichia coli and their functional significance.";
RL Mol. Gen. Genet. 226:367-376(1991).
RN [6]
RP FUNCTION AS AN AMIDASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=11454209; DOI=10.1046/j.1365-2958.2001.02499.x;
RA Heidrich C., Templin M.F., Ursinus A., Merdanovic M., Berger J.,
RA Schwarz H., de Pedro M.A., Holtje J.V.;
RT "Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and
RT antibiotic-induced autolysis of Escherichia coli.";
RL Mol. Microbiol. 41:167-178(2001).
RN [7]
RP SUBCELLULAR LOCATION, AND EXPORT VIA THE TAT-SYSTEM.
RC STRAIN=K12;
RX PubMed=12787347; DOI=10.1046/j.1365-2958.2003.03511.x;
RA Bernhardt T.G., de Boer P.A.;
RT "The Escherichia coli amidase AmiC is a periplasmic septal ring component
RT exported via the twin-arginine transport pathway.";
RL Mol. Microbiol. 48:1171-1182(2003).
RN [8]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [9]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=18390656; DOI=10.1128/jb.00207-08;
RA Uehara T., Park J.T.;
RT "Growth of Escherichia coli: significance of peptidoglycan degradation
RT during elongation and septation.";
RL J. Bacteriol. 190:3914-3922(2008).
CC -!- FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell
CC division. Can also act as powerful autolysin in the presence of murein
CC synthesis inhibitors. {ECO:0000269|PubMed:11454209,
CC ECO:0000269|PubMed:18390656}.
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:0000269|PubMed:12787347}.
CC Note=Distributed throughout the periplasm in all cells.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven. Can also be exported by
CC the Sec system.
CC -!- DISRUPTION PHENOTYPE: Mutants are growing in chains of 3 to 6 cells.
CC {ECO:0000269|PubMed:11454209}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000305}.
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DR EMBL; X75413; CAA53166.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75488.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16318.1; -; Genomic_DNA.
DR EMBL; X63986; CAB57860.1; -; Genomic_DNA.
DR PIR; A36964; A36964.
DR RefSeq; NP_416930.1; NC_000913.3.
DR RefSeq; WP_000102886.1; NZ_LN832404.1.
DR AlphaFoldDB; P36548; -.
DR SMR; P36548; -.
DR BioGRID; 4259617; 388.
DR DIP; DIP-9098N; -.
DR IntAct; P36548; 9.
DR STRING; 511145.b2435; -.
DR jPOST; P36548; -.
DR PaxDb; P36548; -.
DR PRIDE; P36548; -.
DR EnsemblBacteria; AAC75488; AAC75488; b2435.
DR EnsemblBacteria; BAA16318; BAA16318; BAA16318.
DR GeneID; 66673695; -.
DR GeneID; 946916; -.
DR KEGG; ecj:JW2428; -.
DR KEGG; eco:b2435; -.
DR PATRIC; fig|1411691.4.peg.4296; -.
DR EchoBASE; EB1770; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_4_1_6; -.
DR InParanoid; P36548; -.
DR OMA; QIRPVHH; -.
DR PhylomeDB; P36548; -.
DR BioCyc; EcoCyc:NACMURLALAAMI1-MON; -.
DR BioCyc; MetaCyc:NACMURLALAAMI1-MON; -.
DR PRO; PR:P36548; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
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; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF01520; Amidase_3; 1.
DR SMART; SM00646; Ami_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Hydrolase; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..34
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 35..289
FT /note="N-acetylmuramoyl-L-alanine amidase AmiA"
FT /id="PRO_0000006460"
FT DOMAIN 59..273
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000255"
FT REGION 39..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 31412 MW; 614D1E526D9FEFC5 CRC64;
MSTFKPLKTL TSRRQVLKAG LAALTLSGMS QAIAKDELLK TSNGHSKPKA KKSGGKRVVV
LDPGHGGIDT GAIGRNGSKE KHVVLAIAKN VRSILRNHGI DARLTRSGDT FIPLYDRVEI
AHKHGADLFM SIHADGFTNP KAAGASVFAL SNRGASSAMA KYLSERENRA DEVAGKKATD
KDHLLQQVLF DLVQTDTIKN SLTLGSHILK KIKPVHKLHS RNTEQAAFVV LKSPSVPSVL
VETSFITNPE EERLLGTAAF RQKIATAIAE GVISYFHWFD NQKAHSKKR
