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Database: UniProt
Entry: A0A1I0RWM1_9BACT
LinkDB: A0A1I0RWM1_9BACT
Original site: A0A1I0RWM1_9BACT 
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
//
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