ID F2JWL9_MARM1 Unreviewed; 442 AA.
AC F2JWL9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE Flags: Precursor;
GN OrderedLocusNames=Marme_2551 {ECO:0000313|EMBL:ADZ91783.1};
OS Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 /
OS MMB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=717774 {ECO:0000313|EMBL:ADZ91783.1, ECO:0000313|Proteomes:UP000001062};
RN [1] {ECO:0000313|EMBL:ADZ91783.1, ECO:0000313|Proteomes:UP000001062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1
RC {ECO:0000313|Proteomes:UP000001062};
RX PubMed=22675599; DOI=10.4056/sigs.2545743;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Teshima H., Bruce D., Detter C., Tapia R.,
RA Han S., Land M.L., Ivanova N., Mikhailova N., Johnston A.W.,
RA Sanchez-Amat A.;
RT "Complete genome sequence of the melanogenic marine bacterium Marinomonas
RT mediterranea type strain (MMB-1(T)).";
RL Stand. Genomic Sci. 6:63-73(2012).
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};
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DR EMBL; CP002583; ADZ91783.1; -; Genomic_DNA.
DR RefSeq; WP_013661687.1; NZ_CP047696.1.
DR AlphaFoldDB; F2JWL9; -.
DR STRING; 717774.Marme_2551; -.
DR KEGG; mme:Marme_2551; -.
DR PATRIC; fig|717774.3.peg.2636; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_014322_2_3_6; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000001062; Chromosome.
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; cd00118; LysM; 1.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
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 Pfam; PF01476; LysM; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ADZ91783.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001062};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..442
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003284315"
FT DOMAIN 396..439
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 442 AA; 48716 MW; FC24EBB982EA26B1 CRC64;
MYNTFRIKSV VCFVLALFFS MSVYSASVKD IRVAQQDGLT RLVFELDSEA NHRLFLLSSP
DRVVLDLESI GSLSSNVSKN LSKLSSDMMR RLRYAKRDQG ARFVIDLNGK VKAKSSVLSK
NAKYGPRILV ELEYGKKKPV KVIKSVSTIE NAKRDIVVVI DPGHGGKDPG ALGKYKVREK
DVVLSIGKEL AKRINQVKGF KAVLTRSTDV YLKLRQRTKV AREANADILI SIHADAFTKS
SARGASVWAL SLGGKTSEMG RWLAQQEQSS DLVGGISLDD KDQLLAEVLL DMSMNSTIQM
SLDIGESVLA KMTRVAKLHK NTVQQAGFVV LKSPDIPSLL IETGFVSNPT EAKNLSSRTY
RKKLAQAISK GVIDSFSSNP PEGTYLAWKQ KRKVGHTYTV SKGDTLSEIA RRNQVSLKAL
RAANTLKNDV IWIGQKLKIP AS
//
