P36548 (AMIA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetylmuramoyl-L-alanine amidase AmiA
EC=3.5.1.28

Gene names

Name:	amiA
Synonyms:	yfeE
Ordered Locus Names:	b2435, JW2428

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors. Ref.6 Ref.9
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Subcellular location	Periplasm. Note: Distributed throughout the periplasm in all cells. Ref.7
Post-translational modification	Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. Can also be exported by the Sec system.
Disruption phenotype	Mutants are growing in chains of 3 to 6 cells. Ref.6
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Periplasm
Domain	Signal
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	periplasmic space Inferred from direct assay Ref.7. Source: EcoliWiki
Molecular_function	N-acetylmuramoyl-L-alanine amidase activity Inferred from direct assay Ref.6. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 34	34	Tat-type signal Potential
	Chain	35 – 289	255	N-acetylmuramoyl-L-alanine amidase AmiA		PRO_0000006460

Sequences

	Sequence		Length	Mass (Da)
	P36548 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 614D1E526D9FEFC5	FASTA	289	31,412
	10 20 30 40 50 60 MSTFKPLKTL TSRRQVLKAG LAALTLSGMS QAIAKDELLK TSNGHSKPKA KKSGGKRVVV 70 80 90 100 110 120 LDPGHGGIDT GAIGRNGSKE KHVVLAIAKN VRSILRNHGI DARLTRSGDT FIPLYDRVEI 130 140 150 160 170 180 AHKHGADLFM SIHADGFTNP KAAGASVFAL SNRGASSAMA KYLSERENRA DEVAGKKATD 190 200 210 220 230 240 KDHLLQQVLF DLVQTDTIKN SLTLGSHILK KIKPVHKLHS RNTEQAAFVV LKSPSVPSVL 250 260 270 280 VETSFITNPE EERLLGTAAF RQKIATAIAE GVISYFHWFD NQKAHSKKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEM13 mutant." Troup B., Jahn M., Hungerer C., Jahn D. J. Bacteriol. 176:673-680(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Systematic characterization of curved DNA segments randomly cloned from Escherichia coli and their functional significance." Tanaka K., Muramatsu S., Yamada H., Mizuno T. Mol. Gen. Genet. 226:367-376(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
[6]	"Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and antibiotic-induced autolysis of Escherichia coli." Heidrich C., Templin M.F., Ursinus A., Merdanovic M., Berger J., Schwarz H., de Pedro M.A., Holtje J.V. Mol. Microbiol. 41:167-178(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS AN AMIDASE, DISRUPTION PHENOTYPE. Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[7]	"The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway." Bernhardt T.G., de Boer P.A. Mol. Microbiol. 48:1171-1182(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, EXPORT VIA THE TAT-SYSTEM. Strain: K12.
[8]	"Export pathway selectivity of Escherichia coli twin arginine translocation signal peptides." Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B., Palmer T., Georgiou G. J. Biol. Chem. 282:8309-8316(2007) [PubMed] [Europe PMC] [Abstract] Cited for: EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
[9]	"Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation." Uehara T., Park J.T. J. Bacteriol. 190:3914-3922(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: K12.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75413 Genomic DNA. Translation: CAA53166.1. U00096 Genomic DNA. Translation: AAC75488.1. AP009048 Genomic DNA. Translation: BAA16318.1. X63986 Genomic DNA. Translation: CAB57860.1.
PIR	A36964.
RefSeq	NP_416930.1. NC_000913.2. YP_490671.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P36548.
SMR	P36548. Positions 59-272.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9098N.
IntAct	P36548. 9 interactions.
STRING	511145.b2435.
Proteomic databases
PaxDb	P36548.
PRIDE	P36548.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75488; AAC75488; b2435. BAA16318; BAA16318; BAA16318.
GeneID	12930623. 946916.
KEGG	ecj:Y75_p2396. eco:b2435.
PATRIC	32120255. VBIEscCol129921_2530.
Organism-specific databases
EchoBASE	EB1770.
EcoGene	EG11823. amiA.
Phylogenomic databases
eggNOG	COG0860.
HOGENOM	HOG000263827.
KO	K01448.
OMA	RIVMLDP.
ProtClustDB	PRK10319.
Enzyme and pathway databases
BioCyc	EcoCyc:NACMURLALAAMI1-MONOMER. ECOL316407:JW2428-MONOMER. MetaCyc:NACMURLALAAMI1-MONOMER.
Gene expression databases
Genevestigator	P36548.
Family and domain databases
Gene3D	3.40.630.40. 2 hits.
InterPro	IPR002508. CW_Hdrlase/autolysin_cat. IPR006311. TAT_signal. [Graphical view]
Pfam	PF01520. Amidase_3. 1 hit. [Graphical view]
SMART	SM00646. Ami_3. 1 hit. [Graphical view]
PROSITE	PS51318. TAT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMIA_ECOLI

Accession

Primary (citable) accession number: P36548
Secondary accession number(s): P78199

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program