Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P63883

- AMIC_ECOLI

UniProt

P63883 - AMIC_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

N-acetylmuramoyl-L-alanine amidase AmiC

Gene

amiC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 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: EcoCyc

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. FtsZ-dependent cytokinesis Source: EcoCyc
  3. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciEcoCyc:G7458-MONOMER.
ECOL316407:JW5449-MONOMER.
MetaCyc:G7458-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylmuramoyl-L-alanine amidase AmiC (EC:3.5.1.28)
Gene namesi
Name:amiC
Synonyms:ygdN
Ordered Locus Names:b2817, JW5449
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG13086. amiC.

Subcellular locationi

Periplasm 1 Publication
Note: Present throughout the periplasm in non-dividing cells, but localizes almost exclusively to a ring at the site of constriction in dividing cells.

GO - Cellular componenti

  1. outer membrane-bounded periplasmic space Source: EcoCyc
  2. 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 – 3131Tat-type signalPROSITE-ProRule annotationAdd
BLAST
Chaini32 – 417386N-acetylmuramoyl-L-alanine amidase AmiCPRO_0000006465Add
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

PRIDEiP63883.

Expressioni

Gene expression databases

GenevestigatoriP63883.

Interactioni

Protein-protein interaction databases

IntActiP63883. 2 interactions.
STRINGi511145.b2817.

Structurei

Secondary structure

1
417
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 428Combined sources
Beta strandi48 – 569Combined sources
Beta strandi59 – 657Combined sources
Turni66 – 694Combined sources
Beta strandi70 – 778Combined sources
Helixi82 – 854Combined sources
Helixi86 – 905Combined sources
Beta strandi96 – 10712Combined sources
Beta strandi110 – 11910Combined sources
Beta strandi121 – 1288Combined sources
Beta strandi136 – 1449Combined sources
Helixi155 – 1595Combined sources
Turni182 – 1843Combined sources
Beta strandi188 – 1947Combined sources
Helixi211 – 22616Combined sources
Beta strandi232 – 2376Combined sources
Beta strandi239 – 2413Combined sources
Helixi246 – 25510Combined sources
Beta strandi259 – 2657Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi276 – 2827Combined sources
Helixi290 – 30011Combined sources
Helixi302 – 3065Combined sources
Helixi324 – 34320Combined sources
Turni344 – 3463Combined sources
Beta strandi349 – 3535Combined sources
Beta strandi355 – 3573Combined sources
Helixi360 – 3623Combined sources
Beta strandi369 – 3735Combined sources
Helixi380 – 3867Combined sources
Helixi389 – 40618Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BINX-ray2.49A35-417[»]
ProteinModelPortaliP63883.
SMRiP63883. Positions 35-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

N-terminal domain is required and sufficient for targeting to the septal ring.1 Publication

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0860.
HOGENOMiHOG000263827.
InParanoidiP63883.
KOiK01448.
OMAiHKNKVDQ.
OrthoDBiEOG6CP3X3.
PhylomeDBiP63883.

Family and domain databases

Gene3Di3.40.630.40. 2 hits.
InterProiIPR021731. AMIN_dom.
IPR002508. CW_Hdrlase/autolysin_cat.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF01520. Amidase_3. 1 hit.
PF11741. AMIN. 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.

P63883-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGSNTAISR RRLLQGAGAM WLLSVSQVSL AAVSQVVAVR VWPASSYTRV
60 70 80 90 100
TVESNRQLKY KQFALSNPER VVVDIEDVNL NSVLKGMAAQ IRADDPFIKS
110 120 130 140 150
ARVGQFDPQT VRMVFELKQN VKPQLFALAP VAGFKERLVM DLYPANAQDM
160 170 180 190 200
QDPLLALLED YNKGDLEKQV PPAQSGPQPG KAGRDRPIVI MLDPGHGGED
210 220 230 240 250
SGAVGKYKTR EKDVVLQIAR RLRSLIEKEG NMKVYMTRNE DIFIPLQVRV
260 270 280 290 300
AKAQKQRADL FVSIHADAFT SRQPSGSSVF ALSTKGATST AAKYLAQTQN
310 320 330 340 350
ASDLIGGVSK SGDRYVDHTM FDMVQSLTIA DSLKFGKAVL NKLGKINKLH
360 370 380 390 400
KNQVEQAGFA VLKAPDIPSI LVETAFISNV EEERKLKTAT FQQEVAESIL
410
AGIKAYFADG ATLARRG
Length:417
Mass (Da):45,634
Last modified:October 11, 2004 - v1
Checksum:i76F8F733DCCC36D7
GO

Sequence cautioni

The sequence AAB40464.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29581 Genomic DNA. Translation: AAB40464.1. Different initiation.
U00096 Genomic DNA. Translation: AAC75856.2.
AP009048 Genomic DNA. Translation: BAE76886.1.
RefSeqiNP_417294.4. NC_000913.3.
YP_491022.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75856; AAC75856; b2817.
BAE76886; BAE76886; BAE76886.
GeneIDi12932175.
947293.
KEGGiecj:Y75_p2751.
eco:b2817.
PATRICi32121052. VBIEscCol129921_2915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U29581 Genomic DNA. Translation: AAB40464.1 . Different initiation.
U00096 Genomic DNA. Translation: AAC75856.2 .
AP009048 Genomic DNA. Translation: BAE76886.1 .
RefSeqi NP_417294.4. NC_000913.3.
YP_491022.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BIN X-ray 2.49 A 35-417 [» ]
ProteinModelPortali P63883.
SMRi P63883. Positions 35-408.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P63883. 2 interactions.
STRINGi 511145.b2817.

Proteomic databases

PRIDEi P63883.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75856 ; AAC75856 ; b2817 .
BAE76886 ; BAE76886 ; BAE76886 .
GeneIDi 12932175.
947293.
KEGGi ecj:Y75_p2751.
eco:b2817.
PATRICi 32121052. VBIEscCol129921_2915.

Organism-specific databases

EchoBASEi EB2895.
EcoGenei EG13086. amiC.

Phylogenomic databases

eggNOGi COG0860.
HOGENOMi HOG000263827.
InParanoidi P63883.
KOi K01448.
OMAi HKNKVDQ.
OrthoDBi EOG6CP3X3.
PhylomeDBi P63883.

Enzyme and pathway databases

BioCyci EcoCyc:G7458-MONOMER.
ECOL316407:JW5449-MONOMER.
MetaCyc:G7458-MONOMER.

Miscellaneous databases

PROi P63883.

Gene expression databases

Genevestigatori P63883.

Family and domain databases

Gene3Di 3.40.630.40. 2 hits.
InterProi IPR021731. AMIN_dom.
IPR002508. CW_Hdrlase/autolysin_cat.
IPR006311. TAT_signal.
[Graphical view ]
Pfami PF01520. Amidase_3. 1 hit.
PF11741. AMIN. 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. "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.
  3. "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.
  4. "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.
  5. "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, DOMAIN.
    Strain: K12.
  6. "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 nameiAMIC_ECOLI
AccessioniPrimary (citable) accession number: P63883
Secondary accession number(s): Q2MA20, Q46929
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: October 29, 2014
This is version 84 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

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3