ALYS_BPHB3
ID ALYS_BPHB3 Reviewed; 318 AA.
AC P32762;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 02-DEC-2020, entry version 87.
DE RecName: Full=Lytic amidase;
DE EC=3.5.1.28;
DE AltName: Full=N-acetylmuramoyl-L-alanine amidase;
GN Name=HBL;
OS Streptococcus pneumoniae phage HB-3.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=10728;
OH NCBI_TaxID=1313; Streptococcus pneumoniae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1975580; DOI=10.1128/jb.172.9.5064-5070.1990;
RA Romero A., Lopez R., Garcia P.;
RT "Sequence of the Streptococcus pneumoniae bacteriophage HB-3 amidase
RT reveals high homology with the major host autolysin.";
RL J. Bacteriol. 172:5064-5070(1990).
RN [2]
RP PROTEIN SEQUENCE OF 1-21.
RX PubMed=1967150; DOI=10.1128/jvi.64.1.137-142.1990;
RA Romero A., Lopez R., Garcia P.;
RT "Characterization of the pneumococcal bacteriophage HB-3 amidase: cloning
RT and expression in Escherichia coli.";
RL J. Virol. 64:137-142(1990).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; M34652; AAA50574.1; -; Genomic_DNA.
DR PIR; S16016; S16016.
DR SMR; P32762; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; -; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR Pfam; PF01473; Choline_bind_1; 2.
DR Pfam; PF19127; Choline_bind_3; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
DR PROSITE; PS51170; CW; 6.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Hydrolase; Repeat; Secreted.
FT CHAIN 1..318
FT /note="Lytic amidase"
FT /id="PRO_0000164406"
FT DOMAIN 19..151
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT REPEAT 175..194
FT /note="Cell wall-binding 1"
FT REPEAT 196..215
FT /note="Cell wall-binding 2"
FT REPEAT 217..237
FT /note="Cell wall-binding 3"
FT REPEAT 238..257
FT /note="Cell wall-binding 4"
FT REPEAT 258..277
FT /note="Cell wall-binding 5"
FT REPEAT 280..301
FT /note="Cell wall-binding 6"
SQ SEQUENCE 318 AA; 36509 MW; 65B30A9127E58351 CRC64;
MDIDRNRLRT GLPQVGVQPY RQVHAHSTGN RNSTVQNEAD YHWRKDPELG FFSHVVGNFR
IMQVGPVNNG SWDVGGGWNA ETYAAVELIE SHSTKEEFMA DYRLYIELLR NLADEAGLPK
TLDTDDLAGI KTHEYCTNNQ PNNHSDHVDP YPYLASWGIS REQFKQDIEN GLSAATGWQK
NGTGYWYVHS DGSYSKDKFE KINGTWYYFD GSGYMLSDRW KKHTDGNWYY FDQSGEMATG
WKKIADKWYY FDVEGAMKTG WVKYKDTWYY LDAKEGAMVS NAFIQSADGT GWYYLKPDGT
LADKPEFTVE PDGLITVK
