P32762 (ALYS_BPHB3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lytic amidase
EC=3.5.1.28

Alternative name(s):
N-acetylmuramoyl-L-alanine amidase

Gene names

Name:

HBL

Organism

Streptococcus pneumoniae phage HB-3

Taxonomic identifier

10728 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Caudovirales › Siphoviridae

Virus host

Streptococcus pneumoniae [TaxID: 1313]

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
Subcellular location	Secreted Potential.
Sequence similarities	Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. Contains 6 cell wall-binding repeats.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Repeat
Molecular function	Antimicrobial Bacteriolytic enzyme Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW cytolysis Inferred from electronic annotation. Source: UniProtKB-KW 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 – 318	318	Lytic amidase		PRO_0000164406
Regions
	Repeat	175 – 194	20	Cell wall-binding 1
	Repeat	196 – 215	20	Cell wall-binding 2
	Repeat	217 – 237	21	Cell wall-binding 3
	Repeat	238 – 257	20	Cell wall-binding 4
	Repeat	258 – 277	20	Cell wall-binding 5
	Repeat	280 – 301	22	Cell wall-binding 6

Sequences

	Sequence		Length	Mass (Da)
	P32762 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 65B30A9127E58351	FASTA	318	36,509
	10 20 30 40 50 60 MDIDRNRLRT GLPQVGVQPY RQVHAHSTGN RNSTVQNEAD YHWRKDPELG FFSHVVGNFR 70 80 90 100 110 120 IMQVGPVNNG SWDVGGGWNA ETYAAVELIE SHSTKEEFMA DYRLYIELLR NLADEAGLPK 130 140 150 160 170 180 TLDTDDLAGI KTHEYCTNNQ PNNHSDHVDP YPYLASWGIS REQFKQDIEN GLSAATGWQK 190 200 210 220 230 240 NGTGYWYVHS DGSYSKDKFE KINGTWYYFD GSGYMLSDRW KKHTDGNWYY FDQSGEMATG 250 260 270 280 290 300 WKKIADKWYY FDVEGAMKTG WVKYKDTWYY LDAKEGAMVS NAFIQSADGT GWYYLKPDGT 310 LADKPEFTVE PDGLITVK

References

[1]	"Sequence of the Streptococcus pneumoniae bacteriophage HB-3 amidase reveals high homology with the major host autolysin." Romero A., Lopez R., Garcia P. J. Bacteriol. 172:5064-5070(1990) [PubMed: 1975580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Characterization of the pneumococcal bacteriophage HB-3 amidase: cloning and expression in Escherichia coli." Romero A., Lopez R., Garcia P. J. Virol. 64:137-142(1990) [PubMed: 1967150] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M34652 Genomic DNA. Translation: AAA50574.1.
PIR	S16016.
3D structure databases
ProteinModelPortal	P32762.
SMR	P32762. Positions 188-318.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR002502. Amidase_domain. IPR018337. Cell_wall/Cho-bd_repeat. [Graphical view]
Pfam	PF01510. Amidase_2. 1 hit. PF01473. CW_binding_1. 5 hits. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. [Graphical view]
SUPFAM	SSF55846. Amidase_2. 1 hit.
PROSITE	PS51170. CW. 6 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALYS_BPHB3

Accession

Primary (citable) accession number: P32762

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	April 5, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program