(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 115.
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};
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   STRING; 224308.BSU01670; -.
DR   MEROPS; S12.A29; -.
DR   PRIDE; O05213; -.
DR   EnsemblBacteria; CAB11943; CAB11943; BSU01670.
DR   GeneID; 938886; -.
DR   KEGG; bsu:BSU01670; -.
DR   PATRIC; fig|224308.179.peg.173; -.
DR   HOGENOM; HOG000008712; -.
DR   InParanoid; O05213; -.
DR   KO; K21469; -.
DR   OMA; PWAKADR; -.
DR   PhylomeDB; O05213; -.
DR   BioCyc; BSUB:BSU01670-MONOMER; -.
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   InterPro; IPR022849; Pept_S12_YfeW/YbbE-like.
DR   Pfam; PF00144; Beta-lactamase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   1: Evidence at protein level;
DR   PRODOM; O05213.
DR   SWISS-2DPAGE; O05213.
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
//

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