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P26366 (AMIB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. 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 AmiB

EC=3.5.1.28
Gene names
Name:amiB
Ordered Locus Names:STM4358
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length439 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.

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 – 2222 Potential
Chain23 – 439417N-acetylmuramoyl-L-alanine amidase AmiB
PRO_0000006463

Regions

Compositional bias130 – 1356Poly-Pro

Sequences

Sequence LengthMass (Da)Tools
P26366 [UniParc].

Last modified December 19, 2001. Version 2.
Checksum: 01B2BEB753D34DE9

FASTA43946,790
        10         20         30         40         50         60 
MIYRIKNAVI AALILLCAQA GAASLSDIQV SNGEQQARIT LSFIGEPEYA YSQDGKRTVA 

        70         80         90        100        110        120 
LDIRQTGVIQ GLPLQFSGNN LVKTIRAGTP KDAQSLRLLV DLTENGKTEA VKRQNGGNYT 

       130        140        150        160        170        180 
VIFTINADVP PPPPPVVAKR VESAPRPTEP ARNPFKSSDD RLTGVTSSNT VTRPAARASA 

       190        200        210        220        230        240 
GAGDKVVIAI DAGHGGQDPG AIGPGGTREK NVTIAIARKL RTLLNNDPMF KGVLTRDGDY 

       250        260        270        280        290        300 
FISVMGRSDV ARKQNANFLV SIHADAAPNR DATGASVWVL SNRRANSEMA NWLEQHEKQS 

       310        320        330        340        350        360 
ELLGGAGDVL ANSQSDPYLS QAVLDLQFGH SQRVGYDVAT NVLSQLDGVG SLHKRRPEHA 

       370        380        390        400        410        420 
SLGVLRSPDI PSILVETGFI SNHGEERLLA SDRYQQQIAD AIYRGLRKYF AAHPIQSAPQ 

       430 
GGPGQTASTN QPGAITAAN 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"Nucleotide sequence of the Salmonella typhimurium mutL gene required for mismatch repair: homology of MutL to HexB of Streptococcus pneumoniae and to PMS1 of the yeast Saccharomyces cerevisiae."
Mankovich J.A., McIntyre C.A., Walker G.C.
J. Bacteriol. 171:5325-5331(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 340-439.
Strain: LT2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL23178.1.
M29687 Genomic DNA. No translation available.
RefSeqNP_463219.1. NC_003197.1.

3D structure databases

ProteinModelPortalP26366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM4358.

Proteomic databases

PaxDbP26366.
PRIDEP26366.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL23178; AAL23178; STM4358.
GeneID1255884.
KEGGstm:STM4358.
PATRIC32387637. VBISalEnt20916_4582.

Phylogenomic databases

eggNOGCOG0860.
HOGENOMHOG000263828.
KOK01448.
OMALNADPMF.
OrthoDBEOG6CP3X3.
PhylomeDBP26366.

Enzyme and pathway databases

BioCycSENT99287:GCTI-4390-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 nameAMIB_SALTY
AccessionPrimary (citable) accession number: P26366
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 19, 2001
Last modified: July 9, 2014
This is version 89 of the entry and version 2 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