ID D1A9M9_THECD Unreviewed; 694 AA.
AC D1A9M9;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Tcur_3174 {ECO:0000313|EMBL:ACY98715.1};
OS Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Thermomonospora.
OX NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY98715.1, ECO:0000313|Proteomes:UP000001918};
RN [1] {ECO:0000313|EMBL:ACY98715.1, ECO:0000313|Proteomes:UP000001918}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX PubMed=21475583; DOI=10.4056/sigs.1453580;
RA Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL Stand. Genomic Sci. 1:13-22(2011).
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}.
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DR EMBL; CP001738; ACY98715.1; -; Genomic_DNA.
DR RefSeq; WP_012853499.1; NC_013510.1.
DR AlphaFoldDB; D1A9M9; -.
DR STRING; 471852.Tcur_3174; -.
DR KEGG; tcu:Tcur_3174; -.
DR eggNOG; COG5479; Bacteria.
DR HOGENOM; CLU_386692_0_0_11; -.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000001918; 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; 2.60.120.260; Galactose-binding domain-like; 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; 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:UP000001918};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 211..361
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT REGION 32..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 694 AA; 72786 MW; 3A9BB2D6FD851063 CRC64;
MNRRAVIALS TTGVLLSGTV GYIVWPGDSA ATQAEAGPRP GQVRTVPLRT APSDREPPQT
QAPRSPKAPP APAASPVAEL PAARTGPFSM VGVSWDDPGA KLHGSVQVRT RGAASGRWSP
WRTLQIDDHD APDAGSSAER PRRGATKPLW VGPSNGVQIR VTGSGPPPAG LRAELVDPGD
GPRVPQSGPG SGEQPGGAAG QSAGAAAAPA PVIVTRAQWG ADESLVTGSP QYAPAAKVVF
THHSAGGNDY DCAESPAVIR SILLYHVKTN GWNDIGYNFL VDKCGTIFEG RKGGVGKPVI
GAHTYGYNTG SAGVAVLGDF TGVAPSVAAQ KAVARVAAWK LGLHGSDPTG RATVAGKSFN
TISGHRDGVA TACPGELLYG RLGAIRSHAK QWSTPAKPPI VTSITGATES KGTYYTRGAL
TIGWNPAAVS TYEVLLNGKV LARRNGRATW AQVKVPEGAH KLRVRARNLN GTTALSPVYP
VISDVTAPVF RTAPALRVRG GAVGAKGKMP VRLTWKVTDN VRLRSLRATS PTARNFKVSA
TAWATSVKPG VSRKWTLLAA DTLGNNTRAS VTRTAALVHD QSAVRRGRWK VLTTKSYLGR
RALYSKTKGA SVRYAFTGRS VGLIFRRGTA NGAVHIYVDG VKVATIDTKA RSTRYRRIVW
TKSWKRPGRH TVRIVVAGTK GRPAVVTDGI AVIR
//
