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Database: UniProt
Entry: A0A074LP21_9BACL
LinkDB: A0A074LP21_9BACL
Original site: A0A074LP21_9BACL 
ID   A0A074LP21_9BACL        Unreviewed;       517 AA.
AC   A0A074LP21;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=EL26_06935 {ECO:0000313|EMBL:KEO83916.1};
OS   Tumebacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO83916.1, ECO:0000313|Proteomes:UP000027931};
RN   [1] {ECO:0000313|EMBL:KEO83916.1, ECO:0000313|Proteomes:UP000027931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GST4 {ECO:0000313|EMBL:KEO83916.1,
RC   ECO:0000313|Proteomes:UP000027931};
RX   PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA   Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT   "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT   bacterium isolated from cassava wastewater.";
RL   Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013).
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:KEO83916.1}.
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DR   EMBL; JMIR01000007; KEO83916.1; -; Genomic_DNA.
DR   RefSeq; WP_052036075.1; NZ_JMIR01000007.1.
DR   AlphaFoldDB; A0A074LP21; -.
DR   STRING; 1157490.EL26_06935; -.
DR   eggNOG; COG3023; Bacteria.
DR   OrthoDB; 66275at2; -.
DR   Proteomes; UP000027931; 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; 1.10.530.10; -; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
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   Pfam; PF01464; SLT; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 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:UP000027931};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..517
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001697992"
FT   DOMAIN          230..358
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   517 AA;  55998 MW;  0DE18AAAE338A567 CRC64;
     MKKTWVTLLA TTALTFAVTG SALPSYAANS AAKTLATAPN LENAFTAAAK EFGVPKELLM
     AVSYTESRWQ MDAELDTKDH GNGNGLMHLS DKSVKKSLSD TAKALGVNAK QLENDPALNI
     RGGAFVLAQA QKNLGKQLTN NVNDWYEAVA SFEGASDKQS AVLFADEVYR ILKEGTSLTI
     EGGTLSVAAN KAIAPNKGQY AGVTYGLGVT PDATPDYPGA IWNAASTSNY QAATRPTSNP
     INYVIIHDTE GSYSGSINWF KDPTAQVSAH YVVRSSDGQI TQMVQEKDIA WHARSFNTNG
     VGVEHEGYEA QTGWYTDAMY TSSAALVKSI CQRYGIPMDR DHILSHSELW GNDHTDPGAN
     WDWNKYMTKI TGVSKNWTVI NVDDKDTASG AFTLYGSSQY WHPVTGYGLH NEINYTNGNG
     SVIYNYAIWK PTIPTAGNYE VKVFIPSNYA GTTAAKYEIH YNGGTVTKTV NQSAYSNQWV
     SLGTYNFAVG TGGYVKLGDN TGDTNTVAFD TIRFMGQ
//
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