ID A0A1I0RWM1_9BACT Unreviewed; 952 AA.
AC A0A1I0RWM1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN05428988_6130 {ECO:0000313|EMBL:SEW45783.1};
OS Chitinophaga sp. YR573.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEW45783.1, ECO:0000313|Proteomes:UP000198758};
RN [1] {ECO:0000313|EMBL:SEW45783.1, ECO:0000313|Proteomes:UP000198758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR573 {ECO:0000313|EMBL:SEW45783.1,
RC ECO:0000313|Proteomes:UP000198758};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOJF01000003; SEW45783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0RWM1; -.
DR STRING; 1881040.SAMN05428988_6130; -.
DR OrthoDB; 66275at2; -.
DR Proteomes; UP000198758; 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; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 2.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR026444; Secre_tail.
DR InterPro; IPR013693; SpoIID/LytB_N.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
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 Pfam; PF13620; CarboxypepD_reg; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR Pfam; PF08486; SpoIID; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 2.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..952
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011658029"
FT DOMAIN 250..395
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 952 AA; 102308 MW; A43011F915EB0D42 CRC64;
MNRVYLLLKM AVLLLLPYTQ LVAQQQTDNS RLDNYFNEAY RQYPGLPKGI LEAMAYSATH
MTNLQPHEDN CMGMPERFGI FGLVENGKGY FKNNLVEVSK LSNISTAQFK NDVRLQILAT
AKFLSREAGS RKVAAGVESF ATVLESISEI PDDGSAVNAY ARSLYTYDVY DNLQKGFTAA
TLTRAPANVQ LEKIYPAKTL RALKATGVQI DYARDKVISP DNVLDQSAAI DGVSVLSTDY
GPAIFSAAHA NNYTVGRGGV AVTNVTIHTA QGSYAGTISW FKNSTAIVSS HYVIRSSDGQ
VTQMVREKDK AYHVLNHNSY TIGIEHEGYI ADAKWYTTSM YSSSAALVRN ICTKYGISKA
ACFKGAATSG TNYQPKTVRI KGHQHYDGNT HTDPGINWNW KKYAALINPA TVAATKMAIT
VRDQETGFAV ANTAVTVTGP DGTTTRIQTD ENGQTSFDAD KGKYTFSFSA NGYDQIETSF
EGGDETNIAA DISMDRISSS MRIASDDEAI RQVVAANNMI LSGYVRSAVT NAPIAGATVT
AGGRATIFDR NGFFTLTIPV PVTAVTETVA PGVTTLRITR TGFKPYVLNN IRLIADKITV
KVGLTPLTSA SDDQRVATTE EVETYTHGMF DRTAADEAQR TSEYLRIADK DAESAVTAAA
IAVPTSIRVG TSCSCTTCSA VKVMSLEAYV QSGLDNEWIS SWKAASLQAG AVAYRSYGAY
YVKHPVKSNF DIASTTCNQA WGSETATSTI NAAKATAGVV LIKSGAIFRS EYSAENNNAG
CGNGYSGTGS AWPCISDARC AGRTTNGHGR GMCQWGSSFW ASDKTYTWIL NHYYNPGGVT
VQAAATVAAT LAKTEAPKET AIVPTGKLTL FPNPVSGDVV KVGYTLSASA RSAIVLLSDN
TGKVLQRKPV QLIHGYNQFT LDISALKNGI YIVTIKPDLS VISESKKLVV AK
//