ID A0A0L0GW72_9ENTR Unreviewed; 444 AA.
AC A0A0L0GW72;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=GM31_20755 {ECO:0000313|EMBL:KNC93182.1};
OS Trabulsiella odontotermitis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC93182.1, ECO:0000313|Proteomes:UP000037393};
RN [1] {ECO:0000313|EMBL:KNC93182.1, ECO:0000313|Proteomes:UP000037393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12 {ECO:0000313|EMBL:KNC93182.1,
RC ECO:0000313|Proteomes:UP000037393};
RX PubMed=26162887;
RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA Plunkett G.3rd., Perna N.T., Poulsen M.;
RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT Related to Its Association with Fungus-Growing Termites.";
RL Appl. Environ. Microbiol. 81:6577-6588(2015).
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 -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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:KNC93182.1}.
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DR EMBL; JNGI01000062; KNC93182.1; -; Genomic_DNA.
DR RefSeq; WP_049857190.1; NZ_JNGI01000062.1.
DR AlphaFoldDB; A0A0L0GW72; -.
DR STRING; 379893.GCA_001297775_03726; -.
DR PATRIC; fig|379893.4.peg.4211; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000037393; 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; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF6; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIB; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000037393};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..444
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005539193"
FT DOMAIN 254..413
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 424..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 47352 MW; 3B7CE579CF06DB8E CRC64;
MMYRVKSALM AALMLLTLQA TAASLSDIQV SNGDKQARIT FSFMGDPEYS FSQDGRRSVA
LDIKQTGVIQ GLPLQFSGNN LVKSIRSGTP KDDQSLRLVV DLTENGKTRV AKQQNGANYT
VVFTINADAP PPPPPPRVVA KRVEAPAVVS RPSEPARNPF KANNDRITAA TSSNTVTRPA
ASARAVAPGD KVIIAIDAGH GGQDPGAIGP GGTREKNVTI AIARKLRTLL NADPMFKGVM
TRDGDYFISV MGRSDVARKQ NANFLVSIHA DAAPNRGATG ASVWVLSNRR ANSEMASWLE
QHEKQSELLG GAGDVLANSQ SDPYLSQAVL DLQFGHSQRV GYDVAVNVLG QMQRVGNLHK
RHPEHASLGV LRSPDIPSIL VETGFISNTS EERLLASDDF QQQIAEAIYG GLRKYFEAHP
IQSAPQGESA QTASAASPGG ALVN
//
