ID J3TYP9_9ENTR Unreviewed; 522 AA.
AC J3TYP9;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
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 ORFNames=A35E_00230 {ECO:0000313|EMBL:AFP85540.1};
OS secondary endosymbiont of Heteropsylla cubana.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts.
OX NCBI_TaxID=134287 {ECO:0000313|EMBL:AFP85540.1, ECO:0000313|Proteomes:UP000003937};
RN [1] {ECO:0000313|EMBL:AFP85540.1, ECO:0000313|Proteomes:UP000003937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hcub_S {ECO:0000313|EMBL:AFP85540.1};
RX PubMed=22821013; DOI=10.1093/molbev/mss180;
RA Sloan D.B., Moran N.A.;
RT "Genome reduction and co-evolution between the primary and secondary
RT bacterial symbionts of psyllids.";
RL Mol. Biol. Evol. 29:3781-3792(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};
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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DR EMBL; CP003547; AFP85540.1; -; Genomic_DNA.
DR AlphaFoldDB; J3TYP9; -.
DR STRING; 134287.A35E_00230; -.
DR KEGG; sehc:A35E_00230; -.
DR PATRIC; fig|134287.3.peg.221; -.
DR HOGENOM; CLU_014322_2_3_6; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000003937; 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; 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:SF6; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIB; 1.
DR Pfam; PF01520; Amidase_3; 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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000003937};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..522
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003777349"
FT DOMAIN 444..487
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 522 AA; 58395 MW; B0E48F934BAA6412 CRC64;
MIFQFWKMTL VLVSLCAGKS IKAAMLSDID IKNCTNTAKI TFTFNQVPRY NFTLLHNPEA
VILDIYASDA AQDRFPIELS CENIVKSVYL NTPISKQNVR LTFALNHTSK VKSTHNYSSG
RFVLPLNLTK KLPTTLHAKS THDNKVIFSQ SWQSKPSNKL FINETNLVSR SNPNSTPQIQ
QQTRHCHLSV DKKVIVVAID AGHGGQDPGA IGPNGLREKN ITMAIAKKLN ILLEKDAMFK
PVLTRDSDYF VSVKGRSDFA RKKGASVLIS IHADAAPNHR ASGASVWVLS TRRANSEMAA
WLERNEKQSE LLGGTGDLLS RTHPDPYLSH ALLDLQFGYS QRVGYDIALQ ILAQLQQIGP
LHKKLPEHAS LGVLRSPDIP SLLVETSFIT NTREAQLLGN SAYQHKIANA LYLGLRSYFL
AHPIQTFPKV NQSFQKFSSE NNVKYHIVKI NETLFSIARH YKVSINSIRK INKIKEDTIW
IGQQLRIPKN NIVSGASLTS IETDTSTLSV QWDSLIFDRT IN
//
