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Database: UniProt
Entry: K1KKG1_9BURK
LinkDB: K1KKG1_9BURK
Original site: K1KKG1_9BURK 
ID   K1KKG1_9BURK            Unreviewed;       181 AA.
AC   K1KKG1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=HMPREF9465_00189 {ECO:0000313|EMBL:EKB32174.1};
OS   Sutterella wadsworthensis 2_1_59BFAA.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=742823 {ECO:0000313|EMBL:EKB32174.1, ECO:0000313|Proteomes:UP000005835};
RN   [1] {ECO:0000313|EMBL:EKB32174.1, ECO:0000313|Proteomes:UP000005835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2_1_59BFAA {ECO:0000313|EMBL:EKB32174.1,
RC   ECO:0000313|Proteomes:UP000005835};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA   Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA   Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Sutterella wadsworthensis 2_1_59BFAA.";
RL   Submitted (MAY-2012) 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   -!- 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:EKB32174.1}.
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DR   EMBL; ADMG01000007; EKB32174.1; -; Genomic_DNA.
DR   RefSeq; WP_005433238.1; NZ_JH815513.1.
DR   AlphaFoldDB; K1KKG1; -.
DR   STRING; 742823.HMPREF9465_00189; -.
DR   PATRIC; fig|742823.3.peg.186; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_9_5_4; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000005835; 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; 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:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005835}.
FT   DOMAIN          65..177
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   181 AA;  19647 MW;  8A25F81DD721D50A CRC64;
     MSKKLTIVLD PGHGGTDPGA VNGRYKEAEA ALGIANKIAD KLKAKGHRVV LTRTKDQALL
     LQQRCDISNA AKSDAFISIH CNSAENKDAS GIETFKYPGV GGVTKRLAEN IQNGLASSFP
     EEKDRGVKEA KYYVLKHTNA PAALVEVGFI SHDETAEKLF RFSYQDKLAR VIAEGIEKTF
     S
//
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