GenomeNet

Database: UniProt
Entry: A0A1I6G4N6_9RHOB
LinkDB: A0A1I6G4N6_9RHOB
Original site: A0A1I6G4N6_9RHOB 
ID   A0A1I6G4N6_9RHOB        Unreviewed;       379 AA.
AC   A0A1I6G4N6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=SAMN04488005_1072 {ECO:0000313|EMBL:SFR37132.1};
OS   Yoonia tamlensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Yoonia.
OX   NCBI_TaxID=390270 {ECO:0000313|EMBL:SFR37132.1, ECO:0000313|Proteomes:UP000199478};
RN   [1] {ECO:0000313|Proteomes:UP000199478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26879 {ECO:0000313|Proteomes:UP000199478};
RA   Varghese N., Submissions S.;
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FOYP01000001; SFR37132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6G4N6; -.
DR   STRING; 390270.SAMN04488005_1072; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000199478; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199478};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..379
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011665207"
FT   DOMAIN          220..375
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   379 AA;  39915 MW;  BCBE5D48B5D1D9BD CRC64;
     MILRLVCCLI LLCSGAQAQV TIDPARTVVR DGWWQLEVQV GLSKMTPYRL FTLDNPRRLV
     VDFQDVVWPD IAAQTLVSGD RATGLRFGAW GAKWGRMVVD LAGPMAVQEA AMQTGDQGAQ
     LTIILGRSDA QSFAAAAGAP AGADDFAPLV LPRSDASRFR VVIDPGHGGI DPGALREGLT
     EAALMLQLGR EVVNALDALE GVDAVLTREA DVFVPLYARV QMARDAGADL FISLHADALE
     EDAASGASVY TLSTDGGSVA ADRMIARHEA GDLLAGVDLA QQGDSIAALL MDLARDRTGP
     QGHAFAEILI AQMQAAGVRV NSSAHRSGQL AVLSAADFPS VLVEVGFLSN AQDRADLIAP
     QSRARIVTAI VAAVNQFAR
//
DBGET integrated database retrieval system