ID A0A1E7L0P8_9ACTN Unreviewed; 528 AA.
AC A0A1E7L0P8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Peptidoglycan recognition protein family domain-containing protein {ECO:0000259|SMART:SM00701};
GN ORFNames=AN218_20750 {ECO:0000313|EMBL:OEV09754.1};
OS Streptomyces nanshensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=518642 {ECO:0000313|EMBL:OEV09754.1, ECO:0000313|Proteomes:UP000176005};
RN [1] {ECO:0000313|EMBL:OEV09754.1, ECO:0000313|Proteomes:UP000176005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 10429 {ECO:0000313|EMBL:OEV09754.1,
RC ECO:0000313|Proteomes:UP000176005};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEV09754.1}.
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DR EMBL; LJGW01000348; OEV09754.1; -; Genomic_DNA.
DR RefSeq; WP_070018413.1; NZ_LJGW01000348.1.
DR AlphaFoldDB; A0A1E7L0P8; -.
DR PATRIC; fig|518642.10.peg.4610; -.
DR Proteomes; UP000176005; 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 5; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..528
FT /note="Peptidoglycan recognition protein family domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039712489"
FT DOMAIN 332..480
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT REGION 32..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 53617 MW; A3CADCB6B08BED1C CRC64;
MRALLVTSIG IACAGAVLLP LAPTESAEAL LSGKSSTSTG DAAPPVARGS AGGERAGTGT
EARTDAARDG GVSGSTQSLP LRAGGGDKRS GDKLLSAWED DPSGGRRVTS RKVKPFSLVG
VVWKDVSAVP PGRMQVQTRA SGSGKWSSWR TLETHGDGPE SDGRGRSGEK PLGATAPMWT
GDSTAVRVRL LPAAGEKAGG AADRKRAAGE AGLPEGARLE LVDPGDSPGS GSGSRSGADS
GSGSGSGSGA RAGEGGGGGG GDSGSGSEGT ASGGDGGARS DGPRDDDPGQ RPGGVLPELS
RSATRSTYGD DAADATPSDQ DRADDSRIGP RPRIVTRKGW GADENLRERE FAYSKSVKAA
FVHHSAETND YDCADVPAII RGIYRYHVQS SHWRDIGYNF LVDKCGTIYE GRAGGVAKPV
MGAHTLGFNA DTTGIAVLGT YSKAVPSTAA RDALAKLTAW KLGVHGVDAS GKATLTSEGG
TKYRKGSKAT FNAVAGHRDG FTTECPGEKL YGALPGIRTE AGRLQGRR
//