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Protein

N-acetylmuramoyl-L-alanine amidase AmiC

Gene

amiC

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

  • N-acetylmuramoyl-L-alanine amidase activity Source: EcoCyc

GO - Biological processi

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: 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

  • outer membrane-bounded periplasmic space Source: EcoCyc
  • 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Tat-type signalPROSITE-ProRule annotationAdd BLAST31
ChainiPRO_000000646532 – 417N-acetylmuramoyl-L-alanine amidase AmiCAdd BLAST386

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

PaxDbiP63883.
PRIDEiP63883.

Interactioni

Protein-protein interaction databases

BioGridi4261169. 198 interactors.
IntActiP63883. 2 interactors.
STRINGi511145.b2817.

Structurei

Secondary structure

1417
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 42Combined sources8
Beta strandi48 – 56Combined sources9
Beta strandi59 – 65Combined sources7
Turni66 – 69Combined sources4
Beta strandi70 – 77Combined sources8
Helixi82 – 85Combined sources4
Helixi86 – 90Combined sources5
Beta strandi96 – 107Combined sources12
Beta strandi110 – 119Combined sources10
Beta strandi121 – 128Combined sources8
Beta strandi136 – 144Combined sources9
Helixi155 – 159Combined sources5
Turni182 – 184Combined sources3
Beta strandi188 – 194Combined sources7
Helixi211 – 226Combined sources16
Beta strandi232 – 237Combined sources6
Beta strandi239 – 241Combined sources3
Helixi246 – 255Combined sources10
Beta strandi259 – 265Combined sources7
Beta strandi270 – 272Combined sources3
Beta strandi276 – 282Combined sources7
Helixi290 – 300Combined sources11
Helixi302 – 306Combined sources5
Helixi324 – 343Combined sources20
Turni344 – 346Combined sources3
Beta strandi349 – 353Combined sources5
Beta strandi355 – 357Combined sources3
Helixi360 – 362Combined sources3
Beta strandi369 – 373Combined sources5
Helixi380 – 386Combined sources7
Helixi389 – 406Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BINX-ray2.49A35-417[»]
ProteinModelPortaliP63883.
SMRiP63883.
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

eggNOGiENOG4105C5C. Bacteria.
COG0860. LUCA.
HOGENOMiHOG000263827.
InParanoidiP63883.
KOiK01448.
OMAiDLYPQEG.
PhylomeDBiP63883.

Family and domain databases

CDDicd02696. MurNAc-LAA. 1 hit.
Gene3Di3.40.630.40. 2 hits.
InterProiIPR021731. AMIN_dom.
IPR002508. MurNAc-LAA_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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000016907.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75856; AAC75856; b2817.
BAE76886; BAE76886; BAE76886.
GeneIDi947293.
KEGGiecj:JW5449.
eco:b2817.
PATRICi32121052. VBIEscCol129921_2915.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
WP_000016907.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BINX-ray2.49A35-417[»]
ProteinModelPortaliP63883.
SMRiP63883.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261169. 198 interactors.
IntActiP63883. 2 interactors.
STRINGi511145.b2817.

Proteomic databases

PaxDbiP63883.
PRIDEiP63883.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75856; AAC75856; b2817.
BAE76886; BAE76886; BAE76886.
GeneIDi947293.
KEGGiecj:JW5449.
eco:b2817.
PATRICi32121052. VBIEscCol129921_2915.

Organism-specific databases

EchoBASEiEB2895.
EcoGeneiEG13086. amiC.

Phylogenomic databases

eggNOGiENOG4105C5C. Bacteria.
COG0860. LUCA.
HOGENOMiHOG000263827.
InParanoidiP63883.
KOiK01448.
OMAiDLYPQEG.
PhylomeDBiP63883.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP63883.

Family and domain databases

CDDicd02696. MurNAc-LAA. 1 hit.
Gene3Di3.40.630.40. 2 hits.
InterProiIPR021731. AMIN_dom.
IPR002508. MurNAc-LAA_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]
ProtoNetiSearch...

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: November 2, 2016
This is version 95 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

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 one 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.