P26365 (AMIB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	amiB
Synonyms:	yjeD
Ordered Locus Names:	b4169, JW4127

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	445 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.7
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Subcellular location	Periplasm By similarity.
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	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 22	22	Potential
	Chain	23 – 445	423	N-acetylmuramoyl-L-alanine amidase AmiB		PRO_0000006462
Regions
	Compositional bias	130 – 137	8	Poly-Pro

Sequences

	Sequence		Length	Mass (Da)
	P26365 [UniParc]. Last modified July 1, 1993. Version 2. Checksum: C79CC9FD77BFCD38	FASTA	445	47,985
	10 20 30 40 50 60 MMYRIRNWLV ATLLLLCTPV GAATLSDIQV SNGNQQARIT LSFIGDPDYA FSHQSKRTVA 70 80 90 100 110 120 LDIKQTGVIQ GLPLLFSGNN LVKAIRSGTP KDAQTLRLVV DLTENGKTEA VKRQNGSNYT 130 140 150 160 170 180 VVFTINADVP PPPPPPPVVA KRVETPAVVA PRVSEPARNP FKTESNRTTG VISSNTVTRP 190 200 210 220 230 240 AARATANTGD KIIIAIDAGH GGQDPGAIGP GGTREKNVTI AIARKLRTLL NDDPMFKGVL 250 260 270 280 290 300 TRDGDYFISV MGRSDVARKQ NANFLVSIHA DAAPNRSATG ASVWVLSNRR ANSEMASWLE 310 320 330 340 350 360 QHEKQSELLG GAGDVLANSQ SDPYLSQAVL DLQFGHSQRV GYDVATSMIS QLQRIGEIHK 370 380 390 400 410 420 RRPEHASLGV LRSPDIPSVL VETGFISNNS EERLLASDDY QQQLAEAIYK GLRNYFLAHP 430 440 MQSAPQGATA QTASTVTTPD RTLPN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mutL repair gene of Escherichia coli K-12 forms a superoperon with a gene encoding a new cell-wall amidase." Tsui H.-C.T., Zhao G., Feng G., Leung H.-C.E., Winkler M.E. Mol. Microbiol. 11:189-202(1994) [PubMed: 7511774] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R. Nucleic Acids Res. 23:2105-2119(1995) [PubMed: 7610040] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Nonconserved segment of the MutL protein from Escherichia coli K-12 and Salmonella typhimurium." Tsui H.-C.T., Mandavilli B.S., Winkler M.E. Nucleic Acids Res. 20:2379-2379(1992) [PubMed: 1594459] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-445. Strain: K12.
[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: 11454209] [Abstract] Cited for: FUNCTION AS AN AMIDASE. Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
[7]	"Growth of Escherichia coli: significance of peptidoglycan degradation during elongation and septation." Uehara T., Park J.T. J. Bacteriol. 190:3914-3922(2008) [PubMed: 18390656] [Abstract] Cited for: FUNCTION. Strain: K12.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L19346 Unassigned DNA. Translation: AAA20097.1. U14003 Genomic DNA. Translation: AAA97065.1. U00096 Genomic DNA. Translation: AAC77126.1. AP009048 Genomic DNA. Translation: BAE78170.1. Z11831 Genomic DNA. Translation: CAA77851.1.
PIR	S41741.
RefSeq	NP_418590.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P26365.
SMR	P26365. Positions 191-421.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000003235; EBESCP00000003235; EBESCG00000002656. EBESCT00000003236; EBESCP00000003236; EBESCG00000002656. EBESCT00000003237; EBESCP00000003237; EBESCG00000002656. EBESCT00000018149; EBESCP00000017440; EBESCG00000017204.
GeneID	948683.
GenomeReviews	Gene locus JW4127 in contig AP009048_GR. Gene locus b4169 in contig U00096_GR.
KEGG	ecj:JW4127. eco:b4169.
PATRIC	32123911. VBIEscCol129921_4300.
Organism-specific databases
EchoBASE	EB1338.
EcoGene	EG11363. amiB.
Phylogenomic databases
eggNOG	COG0860.
GeneTree	EBGT00050000009921.
HOGENOM	HBG656726.
OMA	IQVSNGD.
PhylomeDB	P26365.
ProtClustDB	PRK10431.
Enzyme and pathway databases
BioCyc	EcoCyc:NACMURLALAAMI2-MONOMER. MetaCyc:NACMURLALAAMI2-MONOMER.
Gene expression databases
Genevestigator	P26365.
Family and domain databases
InterPro	IPR002508. CW_Hdrlase/autolysin_cat. [Graphical view]
Gene3D	G3DSA:3.40.630.40. Cell_wall_OHase/autolysin_cat. 2 hits.
KO	K01448.
Pfam	PF01520. Amidase_3. 1 hit. [Graphical view]
SMART	SM00646. Ami_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMIB_ECOLI

Accession

Primary (citable) accession number: P26365
Secondary accession number(s): Q2M6D6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	July 1, 1993
Last modified:	January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program