AMIE_BACSU
ID AMIE_BACSU Reviewed; 441 AA.
AC O05213; O08069; Q45578;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=N-acetylmuramyl-L-alanine amidase {ECO:0000303|PubMed:20400549};
DE EC=3.5.1.28 {ECO:0000269|PubMed:20400549};
DE Flags: Precursor;
GN Name=amiE {ECO:0000303|PubMed:20400549}; Synonyms=ybbE;
GN OrderedLocusNames=BSU01670;
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;
RX PubMed=9274029; DOI=10.1099/00221287-143-8-2763;
RA Liu H., Haga K., Yasumoto K., Ohashi Y., Yoshikawa H., Takahashi H.;
RT "Sequence and analysis of a 31 kb segment of the Bacillus subtilis
RT chromosome in the area of the rrnH and rrnG operons.";
RL Microbiology 143:2763-2767(1997).
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).
RN [3]
RP SEQUENCE REVISION TO 156-167.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=168;
RX PubMed=20400549; DOI=10.1128/jb.01256-09;
RA Litzinger S., Duckworth A., Nitzsche K., Risinger C., Wittmann V.,
RA Mayer C.;
RT "Muropeptide rescue in Bacillus subtilis involves sequential hydrolysis by
RT beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase.";
RL J. Bacteriol. 192:3132-3143(2010).
CC -!- FUNCTION: Involved in muropeptide recycling. Hydrolyzes the amide bond
CC between N-acetylmuramic acid (MurNAc) and the L-alanine residue of the
CC stem peptide. Cannot hydrolyze muropeptides containing N-
CC acetylglucosamine (GlcNAc) at the non-reducing end.
CC {ECO:0000269|PubMed:20400549}.
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 Evidence={ECO:0000269|PubMed:20400549};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000269|PubMed:20400549}.
CC -!- SIMILARITY: Belongs to the peptidase S12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19500.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA19501.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA19501.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB002150; BAA19500.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AB002150; BAA19501.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB11943.2; -; Genomic_DNA.
DR PIR; A69744; A69744.
DR RefSeq; NP_388048.2; NC_000964.3.
DR RefSeq; WP_003234970.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; O05213; -.
DR SMR; O05213; -.
DR STRING; 224308.BSU01670; -.
DR MEROPS; S12.952; -.
DR PRIDE; O05213; -.
DR EnsemblBacteria; CAB11943; CAB11943; BSU_01670.
DR GeneID; 938886; -.
DR KEGG; bsu:BSU01670; -.
DR PATRIC; fig|224308.179.peg.173; -.
DR eggNOG; COG1680; Bacteria.
DR InParanoid; O05213; -.
DR OMA; AGWAVRY; -.
DR PhylomeDB; O05213; -.
DR BioCyc; BSUB:BSU01670-MON; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000001570; Chromosome.
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:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..441
FT /note="N-acetylmuramyl-L-alanine amidase"
FT /id="PRO_0000036260"
FT CONFLICT 156..167
FT /note="DKIRVIDVLQHQ -> TRYVSLMSSSTN (in Ref. 1; BAA19500/
FT BAA19501)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 441 AA; 49423 MW; 20309AFBE01CADA4 CRC64;
MKTKTLFIFS AILTLSIFAP NETFAQTAGN LIEPKIINAE TAQFSTKKLR KVDQMIERDI
AAGFPGAVLV VVKDGRIIKK AAYGYSKKYE GSELLRRPAK MKTRTMFDLA SNTKMYATNF
ALQRLVSQGK LDVYEKVSAY LPGFKDQPGD LIKGKDKIRV IDVLQHQSGL PSSFYFYTPE
KAGKYYSQER DKTIEYLTKI PLDYQTGTKH VYSDIGYMLL GCIVEKLTGK PLDVYTEQEL
YKPLRLKHTL YNPLQKGFKP KQFAATERMG NTRDGVIQFP NIRTNTLQGE VHDEKAFYSM
DGVSGHAGLF SNADDMAILL QVMLNKGSYR NISLFDQKTA DLFTAPSATD PTFALGWRRN
GSKSMEWMFG PHASENAYGH TGWTGTVTII DPAYNLGIAL LTNKKHTPVI DPEENPNVFE
GDQFPTGSYG SVITAIYEAM E
