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P36548

- AMIA_ECOLI

UniProt

P36548 - AMIA_ECOLI

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Protein

N-acetylmuramoyl-L-alanine amidase AmiA

Gene

amiA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors.2 Publications

Catalytic activityi

Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.

GO - Molecular functioni

  1. N-acetylmuramoyl-L-alanine amidase activity Source: EcoliWiki

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciEcoCyc:NACMURLALAAMI1-MONOMER.
ECOL316407:JW2428-MONOMER.
MetaCyc:NACMURLALAAMI1-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylmuramoyl-L-alanine amidase AmiA (EC:3.5.1.28)
Gene namesi
Name:amiA
Synonyms:yfeE
Ordered Locus Names:b2435, JW2428
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11823. amiA.

Subcellular locationi

Periplasm 1 Publication
Note: Distributed throughout the periplasm in all cells.

GO - Cellular componenti

  1. periplasmic space Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

Mutants are growing in chains of 3 to 6 cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Tat-type signalPROSITE-ProRule annotationAdd
BLAST
Chaini35 – 289255N-acetylmuramoyl-L-alanine amidase AmiAPRO_0000006460Add
BLAST

Post-translational modificationi

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.

Proteomic databases

PaxDbiP36548.
PRIDEiP36548.

Expressioni

Gene expression databases

GenevestigatoriP36548.

Interactioni

Protein-protein interaction databases

DIPiDIP-9098N.
IntActiP36548. 9 interactions.
STRINGi511145.b2435.

Structurei

3D structure databases

ProteinModelPortaliP36548.
SMRiP36548. Positions 59-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0860.
HOGENOMiHOG000263827.
InParanoidiP36548.
KOiK01448.
OMAiSYFNWFD.
OrthoDBiEOG6CP3X3.
PhylomeDBiP36548.

Family and domain databases

Gene3Di3.40.630.40. 2 hits.
InterProiIPR002508. CW_Hdrlase/autolysin_cat.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF01520. Amidase_3. 1 hit.
[Graphical view]
SMARTiSM00646. Ami_3. 1 hit.
[Graphical view]
PROSITEiPS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P36548 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSTFKPLKTL TSRRQVLKAG LAALTLSGMS QAIAKDELLK TSNGHSKPKA
60 70 80 90 100
KKSGGKRVVV LDPGHGGIDT GAIGRNGSKE KHVVLAIAKN VRSILRNHGI
110 120 130 140 150
DARLTRSGDT FIPLYDRVEI AHKHGADLFM SIHADGFTNP KAAGASVFAL
160 170 180 190 200
SNRGASSAMA KYLSERENRA DEVAGKKATD KDHLLQQVLF DLVQTDTIKN
210 220 230 240 250
SLTLGSHILK KIKPVHKLHS RNTEQAAFVV LKSPSVPSVL VETSFITNPE
260 270 280
EERLLGTAAF RQKIATAIAE GVISYFHWFD NQKAHSKKR
Length:289
Mass (Da):31,412
Last modified:June 1, 1994 - v1
Checksum:i614D1E526D9FEFC5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75413 Genomic DNA. Translation: CAA53166.1.
U00096 Genomic DNA. Translation: AAC75488.1.
AP009048 Genomic DNA. Translation: BAA16318.1.
X63986 Genomic DNA. Translation: CAB57860.1.
PIRiA36964.
RefSeqiNP_416930.1. NC_000913.3.
YP_490671.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75488; AAC75488; b2435.
BAA16318; BAA16318; BAA16318.
GeneIDi12930623.
946916.
KEGGiecj:Y75_p2396.
eco:b2435.
PATRICi32120255. VBIEscCol129921_2530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75413 Genomic DNA. Translation: CAA53166.1 .
U00096 Genomic DNA. Translation: AAC75488.1 .
AP009048 Genomic DNA. Translation: BAA16318.1 .
X63986 Genomic DNA. Translation: CAB57860.1 .
PIRi A36964.
RefSeqi NP_416930.1. NC_000913.3.
YP_490671.1. NC_007779.1.

3D structure databases

ProteinModelPortali P36548.
SMRi P36548. Positions 59-272.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9098N.
IntActi P36548. 9 interactions.
STRINGi 511145.b2435.

Proteomic databases

PaxDbi P36548.
PRIDEi P36548.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75488 ; AAC75488 ; b2435 .
BAA16318 ; BAA16318 ; BAA16318 .
GeneIDi 12930623.
946916.
KEGGi ecj:Y75_p2396.
eco:b2435.
PATRICi 32120255. VBIEscCol129921_2530.

Organism-specific databases

EchoBASEi EB1770.
EcoGenei EG11823. amiA.

Phylogenomic databases

eggNOGi COG0860.
HOGENOMi HOG000263827.
InParanoidi P36548.
KOi K01448.
OMAi SYFNWFD.
OrthoDBi EOG6CP3X3.
PhylomeDBi P36548.

Enzyme and pathway databases

BioCyci EcoCyc:NACMURLALAAMI1-MONOMER.
ECOL316407:JW2428-MONOMER.
MetaCyc:NACMURLALAAMI1-MONOMER.

Miscellaneous databases

PROi P36548.

Gene expression databases

Genevestigatori P36548.

Family and domain databases

Gene3Di 3.40.630.40. 2 hits.
InterProi IPR002508. CW_Hdrlase/autolysin_cat.
IPR006311. TAT_signal.
[Graphical view ]
Pfami PF01520. Amidase_3. 1 hit.
[Graphical view ]
SMARTi SM00646. Ami_3. 1 hit.
[Graphical view ]
PROSITEi PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiAMIA_ECOLI
AccessioniPrimary (citable) accession number: P36548
Secondary accession number(s): P78199
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3