XLYA_BACSU
ID XLYA_BACSU Reviewed; 297 AA.
AC P39800;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase XlyA;
DE EC=3.5.1.28;
DE AltName: Full=Autolysin;
DE AltName: Full=Cell wall hydrolase;
DE Flags: Precursor;
GN Name=xlyA; OrderedLocusNames=BSU12810;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / SO113;
RA Krogh S., Joergensen S.T., Diderichsen B., Devine K.M.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7921239; DOI=10.1099/13500872-140-8-1855;
RA Longchamp P.F., Mauel C., Karamata D.;
RT "Lytic enzymes associated with defective prophages of Bacillus subtilis:
RT sequencing and characterization of the region comprising the N-
RT acetylmuramoyl-L-alanine amidase gene of prophage PBSX.";
RL Microbiology 140:1855-1867(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9555893; DOI=10.1128/jb.180.8.2110-2117.1998;
RA Krogh S., Jorgensen S.T., Devine K.M.;
RT "Lysis genes of the Bacillus subtilis defective prophage PBSX.";
RL J. Bacteriol. 180:2110-2117(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-297.
RC STRAIN=168;
RA Devine K.M.;
RT "Sequence of the Bacillus subtilis genome between xlyA and ykoR.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; Z36941; CAA85403.1; -; Genomic_DNA.
DR EMBL; L25924; AAA22645.1; -; Genomic_DNA.
DR EMBL; Z70177; CAA94049.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13138.1; -; Genomic_DNA.
DR EMBL; AJ002571; CAA05561.1; -; Genomic_DNA.
DR PIR; I39938; I39938.
DR RefSeq; NP_389164.1; NC_000964.3.
DR RefSeq; WP_003245230.1; NZ_JNCM01000035.1.
DR PDB; 3HMB; X-ray; 2.70 A; A/B/C=1-154.
DR PDB; 3RDR; X-ray; 2.20 A; A=1-154.
DR PDBsum; 3HMB; -.
DR PDBsum; 3RDR; -.
DR AlphaFoldDB; P39800; -.
DR SMR; P39800; -.
DR STRING; 224308.BSU12810; -.
DR PaxDb; P39800; -.
DR EnsemblBacteria; CAB13138; CAB13138; BSU_12810.
DR GeneID; 939869; -.
DR KEGG; bsu:BSU12810; -.
DR PATRIC; fig|224308.179.peg.1389; -.
DR eggNOG; COG3409; Bacteria.
DR eggNOG; COG5632; Bacteria.
DR InParanoid; P39800; -.
DR OMA; ANNRPGY; -.
DR PhylomeDB; P39800; -.
DR BioCyc; BSUB:BSU12810-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 1.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 1.10.101.10; -; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR Gene3D; 3.40.80.10; -; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF47090; SSF47090; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Competence; Hydrolase;
KW Reference proteome; Secreted; Signal; Sporulation.
FT SIGNAL 1..44
FT /evidence="ECO:0000255"
FT CHAIN 45..297
FT /note="N-acetylmuramoyl-L-alanine amidase XlyA"
FT /id="PRO_0000006457"
FT DOMAIN 45..140
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT DOMAIN 159..203
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:3RDR"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3RDR"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:3RDR"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3RDR"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:3RDR"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3RDR"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:3RDR"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:3RDR"
FT HELIX 102..119
FT /evidence="ECO:0007829|PDB:3RDR"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3RDR"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:3RDR"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:3RDR"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:3RDR"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3RDR"
FT HELIX 146..151
FT /evidence="ECO:0007829|PDB:3RDR"
SQ SEQUENCE 297 AA; 31913 MW; 33DB710059A3EC72 CRC64;
MVNIIQDFIP VGANNRPGYA MTPLYITVHN TANTAVGADA AAHARYLKNP DTTTSWHFTV
DDTEIYQHLP LNENGWHAGD GNGSGNRASI GIEICENADG DFAKATANAQ WLIKTLMAEH
NISLANVVPH KYWSGKECPR KLLDTWDSFK AGIGGGGSQT YVVKQGDTLT SIARAFGVTV
AQLQEWNNIE DPNLIRVGQV LIVSAPSAAE KPELYPLPDG IIQLTTPYTS GEHVFQVQRA
LAALYFYPDK GAVNNGIDGV YGPKTADAVA RFQSVNGLTA DGIYGPATKE KIAAQLS
