ID A0A1Q5TT00_9GAMM Unreviewed; 451 AA.
AC A0A1Q5TT00;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=Xentx_02985 {ECO:0000313|EMBL:OKP03342.1};
OS Xenorhabdus thuongxuanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1873484 {ECO:0000313|EMBL:OKP03342.1, ECO:0000313|Proteomes:UP000186277};
RN [1] {ECO:0000313|EMBL:OKP03342.1, ECO:0000313|Proteomes:UP000186277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=30TX1 {ECO:0000313|EMBL:OKP03342.1,
RC ECO:0000313|Proteomes:UP000186277};
RA Kaempfer P., Tobias N.J., Phan Ke L., Bode H.B., Glaeser S.P.;
RT "Xenorhabdus thuongxuanensis sp. nov. and Xenorhabdus eapokensis sp. nov.,
RT isolated from Steinernema species.";
RL Submitted (SEP-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 -!- 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:OKP03342.1}.
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DR EMBL; MKGR01000026; OKP03342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5TT00; -.
DR Proteomes; UP000186277; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..45
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 46..451
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012660050"
FT DOMAIN 280..438
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 451 AA; 49256 MW; 9F5C199E8CCA2484 CRC64;
MINAFFVNMS LNMFVNEIKK WRAYWVMACA LFFMLSQLVM TAASAATLSN IHVKNGPSEA
VVTLEFIDGH SDYRFFPLHS PERLVVDIRQ SSKIIGLPMH LSGQNLVKLV RSSQSPDAHH
QRVVLELAHK ATATSAVKTS TVKNVGNKSQ VMITLKTKGV ANNSPVSTNH ASQNESKRLL
TNNAQLTGKE TKPVSNHREQ GVQKQAAKSA QGRISRPIVV AIDAGHGGQD PGAIGQRGLK
EKNVTINVAR KLEALLRNDP MFTPVLTRNG DYFISVAGRS EVARKHKANI LVSIHADAAP
NRSARGASVW VLSNRRANSE LGNWLEQHEK QSELLGGAGD ALANGTDPYL SKAVLDLQFG
HSQRVGYDVA MQVLRQLSGI GSLHKRIPEH ASLGVLRSPD IPSILVETGF ISNVSEERLL
GSNQYQEKLA QAIHSGLRYY FLANPLQSAP K
//
