ALYS_STRPN
ID ALYS_STRPN Reviewed; 318 AA.
AC P06653;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Autolysin;
DE EC=3.5.1.28;
DE AltName: Full=Cell wall hydrolase;
DE AltName: Full=Mucopeptide aminohydrolase;
DE AltName: Full=Murein hydrolase;
DE AltName: Full=N-acetylmuramoyl-L-alanine amidase;
GN Name=lytA; OrderedLocusNames=SP_1937;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2875013; DOI=10.1016/0378-1119(86)90215-5;
RA Garcia P., Garcia J.L., Garcia E., Lopez R.;
RT "Nucleotide sequence and expression of the pneumococcal autolysin gene from
RT its own promoter in Escherichia coli.";
RL Gene 43:265-272(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R6 / R800;
RA Martin B.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
CC -!- FUNCTION: Autolysins are involved in some important biological
CC processes such as cell separation, cell-wall turnover, competence for
CC genetic transformation, formation of the flagella and sporulation.
CC Autolysin strictly depends on the presence of choline-containing cell
CC walls for activity.
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 -!- DOMAIN: The C-terminal domain could be responsible for the substrate
CC recognition.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
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DR EMBL; M13812; AAA26917.1; -; Genomic_DNA.
DR EMBL; Z34303; CAA84074.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK76005.1; -; Genomic_DNA.
DR PIR; A25634; A25634.
DR PIR; D95226; D95226.
DR PIR; H98090; H98090.
DR RefSeq; WP_000405234.1; NZ_AKVY01000001.1.
DR PDB; 1GVM; X-ray; 2.80 A; A/B/C/D/E/F=188-318.
DR PDB; 1H8G; X-ray; 2.40 A; A/B=224-318.
DR PDB; 1HCX; X-ray; 2.60 A; A/B=192-318.
DR PDB; 2BML; X-ray; 2.60 A; A/B=193-318.
DR PDB; 4IVV; X-ray; 1.05 A; A=1-180.
DR PDB; 4X36; X-ray; 2.10 A; A=1-318.
DR PDB; 5CTV; X-ray; 1.05 A; A=1-180.
DR PDBsum; 1GVM; -.
DR PDBsum; 1H8G; -.
DR PDBsum; 1HCX; -.
DR PDBsum; 2BML; -.
DR PDBsum; 4IVV; -.
DR PDBsum; 4X36; -.
DR PDBsum; 5CTV; -.
DR AlphaFoldDB; P06653; -.
DR SMR; P06653; -.
DR STRING; 170187.SP_1937; -.
DR DrugBank; DB01912; 2,2':6',2''-Terpyridine Platinum(Ii).
DR DrugBank; DB02613; Capric dimethyl amine oxide.
DR DrugBank; DB03034; D-Levofloxacin.
DR PRIDE; P06653; -.
DR EnsemblBacteria; AAK76005; AAK76005; SP_1937.
DR GeneID; 66807010; -.
DR KEGG; spn:SP_1937; -.
DR eggNOG; COG5263; Bacteria.
DR eggNOG; COG5632; Bacteria.
DR BioCyc; SPNE170187:G1FZB-1992-MON; -.
DR BRENDA; 3.5.1.28; 1960.
DR EvolutionaryTrace; P06653; -.
DR PHI-base; PHI:3152; -.
DR Proteomes; UP000000585; Chromosome.
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:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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; PF01510; Amidase_2; 1.
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 3D-structure; Cell wall biogenesis/degradation; Competence; Hydrolase;
KW Repeat; Secreted; Sporulation.
FT CHAIN 1..318
FT /note="Autolysin"
FT /id="PRO_0000164408"
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"
FT CONFLICT 304
FT /note="K -> R (in Ref. 1; AAA26917 and 2; CAA84074)"
FT /evidence="ECO:0000305"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:4IVV"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:4IVV"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4IVV"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4IVV"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:4IVV"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4IVV"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:4IVV"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:4IVV"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4IVV"
FT HELIX 95..116
FT /evidence="ECO:0007829|PDB:4IVV"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:4IVV"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:4IVV"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:4IVV"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:4IVV"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:4X36"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 287..290
FT /evidence="ECO:0007829|PDB:1H8G"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:1GVM"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:1H8G"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:4X36"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:4X36"
SQ SEQUENCE 318 AA; 36544 MW; 3CA7F3CD132FB502 CRC64;
MEINVSKLRT DLPQVGVQPY RQVHAHSTGN PHSTVQNEAD YHWRKDPELG FFSHIVGNGC
IMQVGPVDNG AWDVGGGWNA ETYAAVELIE SHSTKEEFMT DYRLYIELLR NLADEAGLPK
TLDTGSLAGI KTHEYCTNNQ PNNHSDHVDP YPYLAKWGIS REQFKHDIEN GLTIETGWQK
NDTGYWYVHS DGSYPKDKFE KINGTWYYFD SSGYMLADRW RKHTDGNWYW FDNSGEMATG
WKKIADKWYY FNEEGAMKTG WVKYKDTWYY LDAKEGAMVS NAFIQSADGT GWYYLKPDGT
LADKPEFTVE PDGLITVK
