ID H5UPC9_9MICO Unreviewed; 648 AA.
AC H5UPC9;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=MOPEL_021_00230 {ECO:0000313|EMBL:GAB47587.1};
OS Mobilicoccus pelagius NBRC 104925.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Mobilicoccus.
OX NCBI_TaxID=1089455 {ECO:0000313|EMBL:GAB47587.1, ECO:0000313|Proteomes:UP000004367};
RN [1] {ECO:0000313|EMBL:GAB47587.1, ECO:0000313|Proteomes:UP000004367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 104925 {ECO:0000313|EMBL:GAB47587.1,
RC ECO:0000313|Proteomes:UP000004367};
RA Yoshida Y., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Mobilicoccus pelagius NBRC 104925.";
RL Submitted (FEB-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:GAB47587.1}.
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DR EMBL; BAFE01000020; GAB47587.1; -; Genomic_DNA.
DR AlphaFoldDB; H5UPC9; -.
DR STRING; 1089455.MOPEL_021_00230; -.
DR eggNOG; COG2247; Bacteria.
DR eggNOG; COG5640; Bacteria.
DR Proteomes; UP000004367; 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; 2.130.10.130; Integrin alpha, N-terminal; 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; 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; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF69318; Integrin alpha N-terminal domain; 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:UP000004367};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..648
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003600130"
FT DOMAIN 198..355
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 210..361
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 25..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 648 AA; 67247 MW; 0A4591F2941E54D3 CRC64;
MRLRRLSTLT TAALLAPAFI ALPAQGEPAP KPVETTKETA PLVDPDSPRV GDGDHASTQD
VALAKQTSPE IARTPDLEVL GATGRQEVDE TLAVIGVTWG GSTPLAVQYR TEDARGWSEW
QGIDTGADGE GADAGSGTRN GSDPIVLTGV KAVQARILGA AGESPRNPTL SVIDPGHGDA
DANTDRTAGA AQAAASRPQI RSRAEWGADE SLRRGSPSYG VVRGAIVHHT AGTNNYSPSQ
VPAILRGIYA FHVKDRGWSD IGYNFLVDKW GRVWEGRYGG TSRALVGAQA SGFNSVTMGI
SVMGDYRQVQ PSPAAIDAVT RTIAWKASVH GFDPQGRFSS NGGTYRNVSG HRDVGQTTCP
GLIYGYLPAM ASRAAALKGS ASVGHTGGSA QTGGTARPPV VAAPPAGILN SSDAMLRGSS
GALFAVSPKG AAGITYARSI DKRNWRGYDP VLVTQDISGD TFPDLLTLGS RDGRLYVHPG
TASGVAGRRS LGGGWSSMSH ILAPGDWNGD GRADLLAVQR SNGALYLYPG KGANTFGSRV
KIGSAWGVYR HVVAVGDWDG DRRPDLVGVT PGGQAYLYRG DGRGGFLRSA RKPLGSVAGY
DRFVGMTGSG RLLAIRPNGS AAVLRPAGKG MAATNVAPNF RGLTVFSG
//
