ID A0A133XTW0_9ACTN Unreviewed; 335 AA.
AC A0A133XTW0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-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=HMPREF3192_00922 {ECO:0000313|EMBL:KXB34370.1};
OS Atopobium deltae.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Atopobium.
OX NCBI_TaxID=1393034 {ECO:0000313|EMBL:KXB34370.1, ECO:0000313|Proteomes:UP000070675};
RN [1] {ECO:0000313|Proteomes:UP000070675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DNF00019 {ECO:0000313|Proteomes:UP000070675};
RA Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2016) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:KXB34370.1}.
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DR EMBL; LSCR01000016; KXB34370.1; -; Genomic_DNA.
DR RefSeq; WP_066305622.1; NZ_KQ959496.1.
DR AlphaFoldDB; A0A133XTW0; -.
DR STRING; 1393034.HMPREF3192_00922; -.
DR PATRIC; fig|1393034.3.peg.884; -.
DR OrthoDB; 3186392at2; -.
DR Proteomes; UP000070675; 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; 2.10.270.10; Cholin Binding; 2.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
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; PF19127; Choline_bind_3; 2.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS51170; CW; 4.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000070675};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 13..137
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REPEAT 191..210
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 211..230
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 231..250
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 251..270
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
SQ SEQUENCE 335 AA; 37680 MW; 08259800039E3950 CRC64;
MSYPFKAIYA SPHTYTKGRS GKRVEYIFVH YTSNQGSARN NCLYFSRANR NASAHFFIDG
TGTIYISVPE DSTAWAVGNF DLNQRSISIE VVSDGRDFTS AEISELTWLV QHLMAKYGIP
ASRVYRHHDA ARIATKGKTA SAYKRCPAPY INESKWQALK AQITQGSTTA QGWIKNETGW
WYKRQDASYP ADKWEKINGK WYWFDTHGYM VTGWLKRGDT WYYLDDSGAM VTGWKKINGS
WYYLDDSGAM LTGWQTIEGK KYYFAKAGGQ MATGWLTEGD KYYYADASKD GACIVDCLKE
INGKVYAFDK TGAMLTGTVE VEADQTGALS IKAAG
//
