P81717 (CWHA_ACHLY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetylmuramoyl-L-alanine amidase A
EC=3.5.1.28

Gene names

Name:

cwhA

Organism

Achromobacter lyticus

Taxonomic identifier

224 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Achromobacter

Protein attributes

Sequence length	177 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Antibacterial activity against Gram-positive bacteria M.luteus, S.aureus, E.faecalis and P.acidilactici and Gram-negative bacterium E.coli. Ref.1
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Subcellular location	Secreted.
Biophysicochemical properties	pH dependence: Optimum pH is 8.5.
Mass spectrometry	Molecular mass is 19395.9 Da from positions 1 - 177. Determined by MALDI. Ref.1

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Molecular function	Antibiotic Antimicrobial Hydrolase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	defense response to bacterium Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 177	177	N-acetylmuramoyl-L-alanine amidase A		PRO_0000079618
Regions
	Compositional bias	172 – 175	4	Poly-Gly
Amino acid modifications
	Disulfide bond	114 ↔ 121		Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P81717 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 040D7F5D806C9C53	FASTA	177	19,395
	10 20 30 40 50 60 AVDFGEAIWN PASSSNYSTA SNQTSAVIMH TMEGSYAGSI SWFQNPSAQV SAHYLIRKSD 70 80 90 100 110 120 GQITQMVREY HQAWHAKNHN YYTIGIEHDG RAADAGNWSA AMVNASARLT KSICARRGVN 130 140 150 160 170 CASAWKGPGY DTFHLVPDSV RVKGHGMLSG NENRYDPGKY FPWSNYYNLI NGGGGNP

References

[1]

"Purification, characterization, and primary structure of a novel cell wall hydrolytic amidase, CwhA, from Achromobacter lyticus." Li S., Norioka S., Sakiyama F. J. Biochem. 127:1033-1039(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, DISULFIDE BOND. Strain: M497-1.

Cross-references

Sequence databases
PIR	JC7276.
3D structure databases
ProteinModelPortal	P81717.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.5.1.28. 74.
Family and domain databases
Gene3D	3.40.80.10. 1 hit.
InterPro	IPR002502. Amidase_domain. [Graphical view]
Pfam	PF01510. Amidase_2. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
SUPFAM	SSF55846. Amidase_2. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CWHA_ACHLY

Accession

Primary (citable) accession number: P81717

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	April 3, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program