GenomeNet

Database: UniProt
Entry: A0A090ZFP2_PAEMA
LinkDB: A0A090ZFP2_PAEMA
Original site: A0A090ZFP2_PAEMA 
ID   A0A090ZFP2_PAEMA        Unreviewed;       312 AA.
AC   A0A090ZFP2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=DJ90_401 {ECO:0000313|EMBL:KFN10114.1};
OS   Paenibacillus macerans (Bacillus macerans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=44252 {ECO:0000313|EMBL:KFN10114.1, ECO:0000313|Proteomes:UP000029278};
RN   [1] {ECO:0000313|EMBL:KFN10114.1, ECO:0000313|Proteomes:UP000029278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8244 {ECO:0000313|EMBL:KFN10114.1,
RC   ECO:0000313|Proteomes:UP000029278};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001561};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFN10114.1}.
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DR   EMBL; JMQA01000020; KFN10114.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090ZFP2; -.
DR   STRING; 44252.DJ90_401; -.
DR   PATRIC; fig|44252.3.peg.1633; -.
DR   HOGENOM; CLU_876745_0_0_9; -.
DR   Proteomes; UP000029278; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029278}.
FT   DOMAIN          18..163
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   312 AA;  34702 MW;  170461CE4406895B CRC64;
     MDVTKYNIER RYIAKRSNVR PGTRLKTGTP EFFVAHDTGN PGATADNHYS YFNSQTDRSA
     SAHVFIDDTK ILEIIPTGTG SDPAEKAWHV RYNVTTDNDA FGYDANDAAL GIELCYGGKI
     NFIEAYNRYV WYLAFCCDKW NKNPYTFIPS HKQLDPARKS DCEQALATGG KTLKHLLDDV
     AAEIKSTRSA SSNANTNTNG SFTPLPASIA QSLIDNYVSP AWFASQRKND EAGKTHFHNL
     ANNLRLAAGI PLANDAAAKP LTRLPKSNAQ EIIFRWLSPA WFKAKTEGND PRAQHFHNLA
     NYLRRAAGIP EE
//
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