ID   R7XUM5_9ACTN            Unreviewed;       907 AA.
AC   R7XUM5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=CF8_2982 {ECO:0000313|EMBL:EON23067.1};
OS   Nocardioides sp. CF8.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=110319 {ECO:0000313|EMBL:EON23067.1, ECO:0000313|Proteomes:UP000015971};
RN   [1] {ECO:0000313|EMBL:EON23067.1, ECO:0000313|Proteomes:UP000015971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF8 {ECO:0000313|EMBL:EON23067.1,
RC   ECO:0000313|Proteomes:UP000015971};
RX   PubMed=23833136;
RA   Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT   "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT   of Its Metabolic Capabilities.";
RL   Genome Announc. 1:e00439-e00439(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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
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:EON23067.1}.
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DR   EMBL; ASEP01000091; EON23067.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7XUM5; -.
DR   STRING; 110319.CF8_2982; -.
DR   PATRIC; fig|110319.3.peg.3650; -.
DR   eggNOG; COG2247; Bacteria.
DR   eggNOG; COG2385; Bacteria.
DR   eggNOG; COG5640; Bacteria.
DR   HOGENOM; CLU_014839_0_0_11; -.
DR   OrthoDB; 514320at2; -.
DR   Proteomes; UP000015971; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 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; IPR013517; FG-GAP.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR015510; PGRP.
DR   InterPro; IPR006619; PGRP_domain_met/bac.
DR   PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF13517; FG-GAP_3; 3.
DR   SMART; SM00644; Ami_2; 1.
DR   SMART; SM00701; PGRP; 1.
DR   SUPFAM; SSF69318; Integrin alpha N-terminal domain; 2.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015971};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          250..398
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          263..415
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   REGION          201..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   907 AA;  93461 MW;  4598BE141B383E47 CRC64;
     MRPVQARFVT ACQQLLALGV VLAVLTPAAG VLSLDIVGAP APGGAPALTG ALASATVPTA
     AVPSEVTEVP LTTQSGDARP LAGSTLMRGS AAADHVTSRP QSVSGYGAVG VTWAHGQEIP
     EGGITVLVRT RQDGTWSGWS TIDYHDDHAP DADTAEAAAA RPGTDPVIIG DVDDVQVKAA
     VDGEAATALP ADLKLAVVEP GTAEDTETEA PAESGTQSGS QTQGSYDEEF EDRSEGAISL
     RAARTAPAMP TIYSRAQWGA DESIRNKSSL RYGTVSAGFV HHTVNANDYT EAQVPAIMRS
     IYAYHVKSRG WSDIGYNFLV DRFGRIWEGR YGGVDKNVVG AHTLGYNDYS FAMSAIGNFD
     VVQPPEVMLQ SYGALFAWKL AINGVNPAST AQQVGKSTFQ AISGHRDAGK TACPGRYLYA
     KLPNIRAYAS SAAPAAPAPP PPVQITDPAP QSNLVGAAYP DMVVRSAADN RALILPTGGL
     TSFSKASVTS AKGWANRPEV LVSPDVTGDG VLDLVSTSKQ GVLRIRPGKG NGKFKATSKV
     VKTTKDHTLM TAVGDLNKDG RNDLVARHKG RMVALLGTKK GGFLRSVLGK GLGNYTQLIG
     VGDQNSDGAP DVFARDAKGR LFSYAGSGTG KFGDRSAVPG SWSAYNRITG GADFNGDGRG
     DLVARSAKGK VYIHLAHGDG TFSLPLGPAA NMRSLRSLTS AGSLVGDGAP DLVGVKGNSL
     VVVPHKGTFE LGAPIDTGVV IADADMIINA GDWDRDGAGD VITRRTDGSL WLYRGNGAGQ
     LASPTAIGSG FGGIAGITAV GDVTGDGFPD LLGTPPGGAL SVFAGTGTAI SAGRAVAGRS
     VARTGLPTDL TPFDWVIPVS DIKAKGAGDY LVRQPSTGYL YLYSGTRSGV ARPRFLGEGM
     GAYNLAG
//