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Database: UniProt
Entry: A0A073IEH2_9RHOB
LinkDB: A0A073IEH2_9RHOB
Original site: A0A073IEH2_9RHOB 
ID   A0A073IEH2_9RHOB        Unreviewed;       404 AA.
AC   A0A073IEH2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=DSW25_04380 {ECO:0000313|EMBL:KEJ87950.1};
OS   Sulfitobacter donghicola DSW-25 = KCTC 12864 = JCM 14565.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Sulfitobacter.
OX   NCBI_TaxID=1300350 {ECO:0000313|EMBL:KEJ87950.1, ECO:0000313|Proteomes:UP000027734};
RN   [1] {ECO:0000313|EMBL:KEJ87950.1, ECO:0000313|Proteomes:UP000027734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14565 {ECO:0000313|EMBL:KEJ87950.1,
RC   ECO:0000313|Proteomes:UP000027734};
RA   Lai Q., Hong Z.;
RT   "Sulfitobacter donghicola JCM 14565 Genome Sequencing.";
RL   Submitted (JAN-2014) 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   -!- 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:KEJ87950.1}.
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DR   EMBL; JAMC01000011; KEJ87950.1; -; Genomic_DNA.
DR   RefSeq; WP_025057726.1; NZ_JASF01000005.1.
DR   AlphaFoldDB; A0A073IEH2; -.
DR   STRING; 1300350.Z948_211; -.
DR   eggNOG; COG0860; Bacteria.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000027734; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.60.40.3500; -; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF11741; AMIN; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000027734};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..404
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001689634"
FT   DOMAIN          234..389
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   404 AA;  42988 MW;  54D2806EC9C2D565 CRC64;
     MKTVLLSLIC ALAFASHAVA QGLTAHARVD AASSSITDGW WGRTELSLAL SQGVPFRVFT
     LSDPARLVID FREADFSGVT AGDILPEQGR VSAVRFGAFQ PGWSRLVADL AEPMLPKEIG
     MPVDPNTGRA TLQISLKTAD EADFVAASGA PADPNWAGGF LRAQLPKVPD DGKFTVVIDP
     GHGGIDPGAE REGVSEKHII LSFARTLADA LRRAGVNVVL TRDEDIFVAL QTRVALAHSH
     HADLFISLHA DILRQGGAKG ATVYTLSEGA ADEATQQLVA RHDRSDVLIG MDLTGSDDQV
     AEILLDYARL ETTPRSLALA QHLAAGMAEA GGPMNRRPLR EAGFSVLKSA DIPSVLVEIG
     FLSSDRDLAN LSDPIWRQGM AEGITKSVLA WRDADEANAA LIRQ
//
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