ID M6ZW01_9ACTN Unreviewed; 351 AA.
AC M6ZW01;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Cell wall hydrolase {ECO:0000313|EMBL:EMP10623.2};
GN ORFNames=ISGA_5516 {ECO:0000313|EMBL:EMP10623.2};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:EMP10623.2, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:EMP10623.2, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:EMP10623.2,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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:EMP10623.2}.
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; APHK02000135; EMP10623.2; -; Genomic_DNA.
DR AlphaFoldDB; M6ZW01; -.
DR STRING; 1241906.ISGA_5516; -.
DR OrthoDB; 3268878at2; -.
DR Proteomes; UP000011989; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EMP10623.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000011989};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..351
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005925665"
FT DOMAIN 132..263
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 274..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 351 AA; 35409 MW; 0BBAEF2F10A23079 CRC64;
MTQTRFSRMR MSITAAAVAV ATGAAVLSAV TTAPASAAPA AGTSLAGKTV FLDPGHQGSA
AGHNLSQQVV DGRGGKKDCQ TTGATAVNGT PEHTINWEVA QLVKAGLESQ GARVVLSRPD
DTGWGGCVDE RAAAASRSGA AIAVSLHADS TTTGTDATKK GFHMIVPTLP IPDATVNAVQ
SGEGRKASTV MRDAFVRAGF PTANYAGVVD GIQTRSDIAA VNLTKVPAVF IEMGNLSNPD
DAAALTGKDG QLKYSMAITE GIVNYAKGAA AASTTPSPQN LGAAPAPEAT PQAGDGELSA
VLPFVQKLLG TSDPAEMGQL LLTDGQDASA QVLNAMLVVL YGLFDGKLPI G
//