P63883 (AMIC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	amiC
Synonyms:	ygdN
Ordered Locus Names:	b2817, JW5449

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	417 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.3 Ref.6
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Subcellular location	Periplasm. Note: Present throughout the periplasm in non-dividing cells, but localizes almost exclusively to a ring at the site of constriction in dividing cells. Ref.5
Domain	N-terminal domain is required and sufficient for targeting to the septal ring. Ref.5
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.3
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
Sequence caution	The sequence AAB40464.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

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.5. Source: EcoliWiki
Molecular_function	N-acetylmuramoyl-L-alanine amidase activity Inferred from direct assay Ref.3. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 31	31	Tat-type signal Potential
	Chain	32 – 417	386	N-acetylmuramoyl-L-alanine amidase AmiC		PRO_0000006465

Sequences

	Sequence		Length	Mass (Da)
	P63883 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 76F8F733DCCC36D7	FASTA	417	45,634
	10 20 30 40 50 60 MSGSNTAISR RRLLQGAGAM WLLSVSQVSL AAVSQVVAVR VWPASSYTRV TVESNRQLKY 70 80 90 100 110 120 KQFALSNPER VVVDIEDVNL NSVLKGMAAQ IRADDPFIKS ARVGQFDPQT VRMVFELKQN 130 140 150 160 170 180 VKPQLFALAP VAGFKERLVM DLYPANAQDM QDPLLALLED YNKGDLEKQV PPAQSGPQPG 190 200 210 220 230 240 KAGRDRPIVI MLDPGHGGED SGAVGKYKTR EKDVVLQIAR RLRSLIEKEG NMKVYMTRNE 250 260 270 280 290 300 DIFIPLQVRV AKAQKQRADL FVSIHADAFT SRQPSGSSVF ALSTKGATST AAKYLAQTQN 310 320 330 340 350 360 ASDLIGGVSK SGDRYVDHTM FDMVQSLTIA DSLKFGKAVL NKLGKINKLH KNQVEQAGFA 370 380 390 400 410 VLKAPDIPSI LVETAFISNV EEERKLKTAT FQQEVAESIL AGIKAYFADG ATLARRG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"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.
[4]	"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.
[5]	"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, DOMAIN. Strain: K12.
[6]	"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	U29581 Genomic DNA. Translation: AAB40464.1. Different initiation. U00096 Genomic DNA. Translation: AAC75856.2. AP009048 Genomic DNA. Translation: BAE76886.1.
RefSeq	NP_417294.4. NC_000913.2. YP_491022.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P63883.
SMR	P63883. Positions 190-406.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63883. 2 interactions.
STRING	511145.b2817.
Proteomic databases
PRIDE	P63883.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75856; AAC75856; b2817. BAE76886; BAE76886; BAE76886.
GeneID	12932175. 947293.
KEGG	ecj:Y75_p2751. eco:b2817.
PATRIC	32121052. VBIEscCol129921_2915.
Organism-specific databases
EchoBASE	EB2895.
EcoGene	EG13086. amiC.
Phylogenomic databases
eggNOG	COG0860.
HOGENOM	HOG000263827.
KO	K01448.
OMA	YRDEMAD.
ProtClustDB	CLSK880499.
Enzyme and pathway databases
BioCyc	EcoCyc:G7458-MONOMER. ECOL316407:JW5449-MONOMER. MetaCyc:G7458-MONOMER.
Gene expression databases
Genevestigator	P63883.
Family and domain databases
Gene3D	3.40.630.40. 2 hits.
InterPro	IPR021731. AMIN_dom. IPR002508. CW_Hdrlase/autolysin_cat. IPR006311. TAT_signal. [Graphical view]
Pfam	PF01520. Amidase_3. 1 hit. PF11741. AMIN. 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

AMIC_ECOLI

Accession

Primary (citable) accession number: P63883
Secondary accession number(s): Q2MA20, Q46929

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program