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P33772 (AMIA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetylmuramoyl-L-alanine amidase AmiA

EC=3.5.1.28
Gene names
Name:amiA
Ordered Locus Names:STM2450
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cell-wall hydrolase involved in septum cleavage during cell division By similarity.

Catalytic activity

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

Subcellular location

Periplasm By similarity.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.

Sequence similarities

Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.

Ontologies

Keywords
   Biological processCell wall biogenesis/degradation
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpeptidoglycan catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylmuramoyl-L-alanine amidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434Tat-type signal Potential
Chain35 – 289255N-acetylmuramoyl-L-alanine amidase AmiA
PRO_0000006461

Sequences

Sequence LengthMass (Da)Tools
P33772 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 8FCC21089D56F671

FASTA28931,659
        10         20         30         40         50         60 
MSTFKLLKTL TSRRQVLKTG LAALTLSGMS HAVAKEETLK TSNGHSKPKT KKTGSKRLVM 

        70         80         90        100        110        120 
LDPGHGGIDT GAIGRNGSQE KHVVLAIAKN VRAILRNHGI DARLTRTGDT FIPLYDRVEI 

       130        140        150        160        170        180 
AHKHGADLFM SIHADGFTNP KAAGASVFAL SNRGASSAMA KYLSERENRA DEVAGKKATD 

       190        200        210        220        230        240 
RDHLLQQVLF DLVQTDTIKN SLTLGSHILK KIKPIHKLHS RTTEQAAFVV LKSPSIPSVL 

       250        260        270        280 
VETSFITNPE EERLLGTTAF RQKIATAIAN GIISYFHWFD NQKAHTKKR 

« Hide

References

« Hide 'large scale' references
[1]"An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium."
Xu K., Elliott T.
J. Bacteriol. 175:4990-4999(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19503 Genomic DNA. Translation: AAA27138.1.
AE006468 Genomic DNA. Translation: AAL21344.1.
PIRA53302.
RefSeqNP_461385.1. NC_003197.1.

3D structure databases

ProteinModelPortalP33772.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM2450.

Proteomic databases

PaxDbP33772.
PRIDEP33772.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL21344; AAL21344; STM2450.
GeneID1253972.
KEGGstm:STM2450.
PATRIC32383531. VBISalEnt20916_2588.

Phylogenomic databases

eggNOGCOG0860.
HOGENOMHOG000263827.
KOK01448.
OMASAMARYL.
OrthoDBEOG6CP3X3.
ProtClustDBPRK10319.

Enzyme and pathway databases

BioCycSENT99287:GCTI-2466-MONOMER.

Family and domain databases

Gene3D3.40.630.40. 2 hits.
InterProIPR002508. CW_Hdrlase/autolysin_cat.
[Graphical view]
PfamPF01520. Amidase_3. 1 hit.
[Graphical view]
SMARTSM00646. Ami_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAMIA_SALTY
AccessionPrimary (citable) accession number: P33772
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: February 19, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families