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
//