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
//