ID K9CJT5_9FIRM Unreviewed; 162 AA.
AC K9CJT5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-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=HMPREF9161_00803 {ECO:0000313|EMBL:EKU72118.1};
OS Selenomonas sp. F0473.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=999423 {ECO:0000313|EMBL:EKU72118.1, ECO:0000313|Proteomes:UP000009883};
RN [1] {ECO:0000313|EMBL:EKU72118.1, ECO:0000313|Proteomes:UP000009883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0473 {ECO:0000313|EMBL:EKU72118.1,
RC ECO:0000313|Proteomes:UP000009883};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Blanton J.M., Baranova O.V.,
RA Mathney J., Dewhirst F.E., Izard J., Tanner A.C., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas sp. Oral taxon 133 strain F0473.";
RL Submitted (SEP-2012) 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 -!- 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:EKU72118.1}.
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DR EMBL; AGZT01000003; EKU72118.1; -; Genomic_DNA.
DR RefSeq; WP_009728407.1; NZ_JH992902.1.
DR AlphaFoldDB; K9CJT5; -.
DR STRING; 999423.HMPREF9161_00803; -.
DR PATRIC; fig|999423.3.peg.836; -.
DR eggNOG; COG3023; Bacteria.
DR HOGENOM; CLU_079366_2_0_9; -.
DR OrthoDB; 9812621at2; -.
DR Proteomes; UP000009883; 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; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
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 Reference proteome {ECO:0000313|Proteomes:UP000009883};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 4..136
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 11..142
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 162 AA; 17704 MW; 2AF5FC2DA6D6B5E0 CRC64;
MQRVNIKDTG LDFGALSKRP TTDQIVIHHT GNPYDDDLSA AEIHASHRAK GWSGIGYHYV
VRKDASIEAG RPHWTVGAHA YEHNNHTIGI HVCGNFELAE PTGAQIEALS MLIANLCVDY
GLPIDGDHVV GHRDLMPTAC PGANLYAMLP EIRGKGNWYA NN
//
