ID U3U5V3_9GAMM Unreviewed; 424 AA.
AC U3U5V3;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=BMSBPS_0747 {ECO:0000313|EMBL:AKC32518.1}, HHS_02750
GN {ECO:0000313|EMBL:BAO00245.1};
OS Candidatus Pantoea carbekii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1235990 {ECO:0000313|EMBL:BAO00245.1, ECO:0000313|Proteomes:UP000016900};
RN [1] {ECO:0000313|EMBL:BAO00245.1, ECO:0000313|Proteomes:UP000016900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kobayashi H., Fujii-Muramatsu R., Takeishi K., Noda H.;
RT "Genome sequence of the symbiont of the pentatomidae stink bug Halyomorpha
RT halys.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKC32518.1, ECO:0000313|Proteomes:UP000060036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=US {ECO:0000313|EMBL:AKC32518.1,
RC ECO:0000313|Proteomes:UP000060036};
RX PubMed=25587021; DOI=10.1093/gbe/evv006;
RA Kenyon L.J., Meulia T., Sabree Z.L.;
RT "Habitat visualization and genomic analysis of "Candidatus Pantoea
RT carbekii," the primary symbiont of the brown marmorated stink bug.";
RL Genome Biol. Evol. 7:620-635(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}.
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DR EMBL; CP010907; AKC32518.1; -; Genomic_DNA.
DR EMBL; AP012554; BAO00245.1; -; Genomic_DNA.
DR RefSeq; WP_022564264.1; NZ_CP010907.1.
DR AlphaFoldDB; U3U5V3; -.
DR STRING; 1235990.BMSBPS_0747; -.
DR KEGG; hhs:HHS_02750; -.
DR KEGG; pck:BMSBPS_0747; -.
DR PATRIC; fig|1235990.3.peg.276; -.
DR eggNOG; COG0860; Bacteria.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000016900; Chromosome.
DR Proteomes; UP000060036; 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; 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:UP000016900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..424
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033706988"
FT DOMAIN 243..402
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 424 AA; 48983 MW; 0BA3AB8EB3643AE8 CRC64;
MLRIKIFLLI ILCSFSNSIF AAILYGINVE NSDTLAEITL NFKGKPTYFF FLRDHPYCLV
LDMRQNGMIT GLPYHFKGKN IIQRIRNSRL KSKQKIRLIF ELTHKAKTYV KIIHKNHAYR
MTFKIHAIER IRPNRKLQKI SSNIEHFKYR KIFYNKLIST RFIDNTLYNF KKKVRRHRNL
VIVAIDAGHG GQDPGASSQK GLHEKNITIV IARKLKALMD RDNIFKGILT RNGDYFISVK
GRSEIARKSH ANFLISIHVD SAHNHSVTGA SVWVLSNRRA KIEMAHLLAK KEKQLKLLGG
LGALLINRQI DQYLSQTILD LQFDYSKRVG YEVALKVLQQ LNYVTSLHKR LPQHASLGIL
RSPDIPSLLV EIGFISNSRE ARLINTKIYQ KKIAQSIYKG LRNYFLVHSI QSMIDNPYSS
LNSV
//
