ID A0A1V9FVP1_9BACT Unreviewed; 533 AA.
AC A0A1V9FVP1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=A3860_29160 {ECO:0000313|EMBL:OQP62429.1};
OS Niastella vici.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Niastella.
OX NCBI_TaxID=1703345 {ECO:0000313|EMBL:OQP62429.1, ECO:0000313|Proteomes:UP000192796};
RN [1] {ECO:0000313|EMBL:OQP62429.1, ECO:0000313|Proteomes:UP000192796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ57 {ECO:0000313|EMBL:OQP62429.1,
RC ECO:0000313|Proteomes:UP000192796};
RA Chen L., Wang D., Yang S., Wang G.;
RT "Niastella vici sp. nov., isolated from farmland soil.";
RL Submitted (MAR-2016) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:OQP62429.1}.
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DR EMBL; LVYD01000051; OQP62429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9FVP1; -.
DR STRING; 1703345.A3860_29160; -.
DR Proteomes; UP000192796; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000192796};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..533
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013365829"
FT DOMAIN 258..404
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 426..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 57579 MW; A7A573BB2B7C8047 CRC64;
MITRRSLCGL FCSLVLGTQL SAQQSEQDFS GYFAEAYRLY PSIPKGVLEA TAYSASHMNN
LAPQTDGDGD EVGMPQRFGI FGLIEDGKGY FKNNLTAVCS LSGITPERFK KDVHLQILAV
AKFLNREAGV QSLAANSTPE SFSVALDRLS EIPDDGSAIN KYAHSLYTYD VFHHLQKGFT
SPGIKLPARS VQFEKIYPAK TLRLLRTPGV QVNVDQGRIA ADDAALSTEP TSEANGISDV
AAAQGPDYPS AKWDQASTSN FTVGRGGAAI TNVVVHTTEG SYSGTISWFN NPSAKVSAHY
VIRSSDGQVT QMVREKDKAW HVLNHNGYTI GIEHEGYVAN GNTWYTTAMY KSSAALVRDI
CRGRNIDGKK CFRGPATAGT NPQPVTVRIK GHQHYSGNTH TDPGKYWNWT KYANLISPPS
VAAALPESAD DEVTAEPAPS QSAKADGALK ITPNPVTGSS VTIEYMLQNA SQPANIVIAN
NYGNVAQQRS VVLQHGINRL TIPVSNLKTG VYNITIRLST TGKSESRQLI VVK
//
