ID A0A0G1W6L6_9BACT Unreviewed; 748 AA.
AC A0A0G1W6L6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=UY52_C0029G0004 {ECO:0000313|EMBL:KKW14416.1};
OS Parcubacteria group bacterium GW2011_GWC2_49_9.
OC Bacteria.
OX NCBI_TaxID=1618934 {ECO:0000313|EMBL:KKW14416.1, ECO:0000313|Proteomes:UP000034059};
RN [1] {ECO:0000313|EMBL:KKW14416.1, ECO:0000313|Proteomes:UP000034059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKW14416.1}.
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DR EMBL; LCQH01000029; KKW14416.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1W6L6; -.
DR PATRIC; fig|1618934.3.peg.1130; -.
DR Proteomes; UP000034059; Unassembled WGS sequence.
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; 2.60.40.10; Immunoglobulins; 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; IPR013783; Ig-like_fold.
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 SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 189..345
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 208..361
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 748 AA; 81374 MW; 97FE386B97B6E437 CRC64;
MKRQAVKKSV IFIILGVAMA AGIFVLEPVG RASSGEEVIA KTMTISSSLS NTEVVQPQYV
RSSVLYAEFP FIGIGMSWDG ELPESYKVSI RARAKDGGWG EWMDVSPQID FPDGWTAADG
KNYAQPIFFP ESDAWQYSLW TLEDEHLPRI EDITFRYFDS REERTTKANI GDWLRSLISG
ASAVTPIGVD VVSRAEWGAN ESLGQTSSGG PIWEPEYAQP AKIIIHHTAG SDGGNDPKSI
VRGIYYWHTV SLGWGDIGYN YLIDKNGVIY EGREGGDGVV GGHAYNEAKD IGYNRGSIGI
AVLGQYESGV PTAAAIDALT RLSASLGVRF GLEPDGNGFF VDETLPNVFG HKEVDNTLCP
GENLGSNVDT IRSEAQKLFE AAGGYAQSTN TLKASFVRQS VQPVKIPSGS QKQLWVEFKN
TGTVTWRSYA QPAFKIVSAN VSSNLMAGGA ASGNTAVLDT PNVAPGEVGR FFYTLKAPND
TVEANDTFVL KAGSATVAIA SFNVTVQVTG LSYAAAARDI EILPATFSRA RNTTVVRFTN
LGTQAWKRGE VKLGIYDLGN RGSRYQDASW PDDNGMFDFE ELEVVSGGTA TFRFVLLSPD
EPGLYLNVYR VSGPDGLAQK EDRSVTRVDS PYEAKFISHT VPAAMLNIWR PAVTLTFKNT
GVMPWDRSVG LQVVDLGDTD SQFANSNWDD IRIATHLNEA QVNPGEFGTF TLRLYPPQNS
GLYLNIMRVF KDGRPIKGGT FNAITRVD
//