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Protein

N-acetylmuramoyl-L-alanine amidase AmiB

Gene

amiB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 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:NACMURLALAAMI2-MONOMER.
ECOL316407:JW4127-MONOMER.
MetaCyc:NACMURLALAAMI2-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylmuramoyl-L-alanine amidase AmiB (EC:3.5.1.28)
Gene namesi
Name:amiB
Synonyms:yjeD
Ordered Locus Names:b4169, JW4127
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11363. amiB.

Subcellular locationi

  1. Periplasm By similarity

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 445423N-acetylmuramoyl-L-alanine amidase AmiBPRO_0000006462Add
BLAST

Proteomic databases

PaxDbiP26365.

Expressioni

Gene expression databases

GenevestigatoriP26365.

Interactioni

Protein-protein interaction databases

STRINGi511145.b4169.

Structurei

3D structure databases

ProteinModelPortaliP26365.
SMRiP26365. Positions 192-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi130 – 1378Poly-Pro

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0860.
HOGENOMiHOG000263828.
InParanoidiP26365.
KOiK01448.
OMAiQPVYAFF.
OrthoDBiEOG6CP3X3.
PhylomeDBiP26365.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

P26365-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMYRIRNWLV ATLLLLCTPV GAATLSDIQV SNGNQQARIT LSFIGDPDYA
60 70 80 90 100
FSHQSKRTVA LDIKQTGVIQ GLPLLFSGNN LVKAIRSGTP KDAQTLRLVV
110 120 130 140 150
DLTENGKTEA VKRQNGSNYT VVFTINADVP PPPPPPPVVA KRVETPAVVA
160 170 180 190 200
PRVSEPARNP FKTESNRTTG VISSNTVTRP AARATANTGD KIIIAIDAGH
210 220 230 240 250
GGQDPGAIGP GGTREKNVTI AIARKLRTLL NDDPMFKGVL TRDGDYFISV
260 270 280 290 300
MGRSDVARKQ NANFLVSIHA DAAPNRSATG ASVWVLSNRR ANSEMASWLE
310 320 330 340 350
QHEKQSELLG GAGDVLANSQ SDPYLSQAVL DLQFGHSQRV GYDVATSMIS
360 370 380 390 400
QLQRIGEIHK RRPEHASLGV LRSPDIPSVL VETGFISNNS EERLLASDDY
410 420 430 440
QQQLAEAIYK GLRNYFLAHP MQSAPQGATA QTASTVTTPD RTLPN
Length:445
Mass (Da):47,985
Last modified:July 1, 1993 - v2
Checksum:iC79CC9FD77BFCD38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS41741.
RefSeqiNP_418590.1. NC_000913.3.
YP_492311.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77126; AAC77126; b4169.
BAE78170; BAE78170; BAE78170.
GeneIDi12934195.
948683.
KEGGiecj:Y75_p4055.
eco:b4169.
PATRICi32123911. VBIEscCol129921_4300.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS41741.
RefSeqiNP_418590.1. NC_000913.3.
YP_492311.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP26365.
SMRiP26365. Positions 192-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi511145.b4169.

Proteomic databases

PaxDbiP26365.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77126; AAC77126; b4169.
BAE78170; BAE78170; BAE78170.
GeneIDi12934195.
948683.
KEGGiecj:Y75_p4055.
eco:b4169.
PATRICi32123911. VBIEscCol129921_4300.

Organism-specific databases

EchoBASEiEB1338.
EcoGeneiEG11363. amiB.

Phylogenomic databases

eggNOGiCOG0860.
HOGENOMiHOG000263828.
InParanoidiP26365.
KOiK01448.
OMAiQPVYAFF.
OrthoDBiEOG6CP3X3.
PhylomeDBiP26365.

Enzyme and pathway databases

BioCyciEcoCyc:NACMURLALAAMI2-MONOMER.
ECOL316407:JW4127-MONOMER.
MetaCyc:NACMURLALAAMI2-MONOMER.

Miscellaneous databases

PROiP26365.

Gene expression databases

GenevestigatoriP26365.

Family and domain databases

Gene3Di3.40.630.40. 2 hits.
InterProiIPR002508. CW_Hdrlase/autolysin_cat.
[Graphical view]
PfamiPF01520. Amidase_3. 1 hit.
[Graphical view]
SMARTiSM00646. Ami_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  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. "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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12.

Entry informationi

Entry nameiAMIB_ECOLI
AccessioniPrimary (citable) accession number: P26365
Secondary accession number(s): Q2M6D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 1, 1993
Last modified: January 7, 2015
This is version 109 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.