BLYA_BACSU
ID BLYA_BACSU Reviewed; 367 AA.
AC O31982;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase BlyA;
DE EC=3.5.1.28;
DE AltName: Full=Autolysin;
DE AltName: Full=Cell wall hydrolase;
GN Name=blyA; Synonyms=yomC; OrderedLocusNames=BSU21410;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=168;
RX PubMed=9579063; DOI=10.1099/00221287-144-4-885;
RA Regamey A., Karamata D.;
RT "The N-acetylmuramoyl-L-alanine amidase encoded by the Bacillus subtilis
RT 168 prophage SP beta.";
RL Microbiology 144:885-893(1998).
RN [2]
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).
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 Involved in prophage SP-beta-mediated cell lysis.
CC {ECO:0000269|PubMed:9579063}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF021803; AAC38300.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14059.1; -; Genomic_DNA.
DR RefSeq; NP_390024.1; NC_000964.3.
DR RefSeq; WP_004399108.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O31982; -.
DR SMR; O31982; -.
DR STRING; 224308.BSU21410; -.
DR PaxDb; O31982; -.
DR PRIDE; O31982; -.
DR EnsemblBacteria; CAB14059; CAB14059; BSU_21410.
DR GeneID; 939130; -.
DR KEGG; bsu:BSU21410; -.
DR PATRIC; fig|224308.179.peg.2338; -.
DR eggNOG; COG5632; Bacteria.
DR OMA; VNKYTRP; -.
DR BioCyc; BSUB:BSU21410-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; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; -; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR003646; SH3-like_bac-type.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
DR PROSITE; PS51781; SH3B; 2.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Competence; Hydrolase;
KW Reference proteome; Secreted; Sporulation.
FT CHAIN 1..367
FT /note="N-acetylmuramoyl-L-alanine amidase BlyA"
FT /id="PRO_0000164416"
FT DOMAIN 24..158
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT DOMAIN 202..271
FT /note="SH3b 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT DOMAIN 298..367
FT /note="SH3b 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT REGION 178..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 39629 MW; 20D8BA91DF6A982A CRC64;
MSVFTNSYIP VNKYTRPGLK LQGVKKCVLH YTANPGAGAD NHRRYFSNAQ VYASAHIFVD
KAEAICIIPL NEVAYHANDI QQRDSAGNPY RGVAALKPNA NFLSIGVEMC LEKDGSFHSD
TVERTEDVFV ELCNKFGLDP IDDIVRHYDI THKNCPAPWV SNSQKFVDFK NRVKAKMSGK
SVSKASPTKP TTSSPSSSSA VSGSLKSKVD GLRFYSKPSW EDKDVVGTVN KGIGFPTVVE
KVKVGSAYQY KVKNSKGTTY YITASDKYVD VTGSVKTSSS APKTTSTSSS SSSIKSVGKI
KIVGVSSAAI VMDKPDRNSS KNIGTVKLGS TISISGSVKG KNNSNGYWEV IYKGKRGYIS
GQFGSTI
