ID F3QII0_9BURK Unreviewed; 476 AA.
AC F3QII0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-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=HMPREF9439_00729 {ECO:0000313|EMBL:EGG56797.1};
OS Parasutterella excrementihominis YIT 11859.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Parasutterella.
OX NCBI_TaxID=762966 {ECO:0000313|EMBL:EGG56797.1, ECO:0000313|Proteomes:UP000005156};
RN [1] {ECO:0000313|EMBL:EGG56797.1, ECO:0000313|Proteomes:UP000005156}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11859 {ECO:0000313|EMBL:EGG56797.1,
RC ECO:0000313|Proteomes:UP000005156};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2011) 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:EGG56797.1}.
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DR EMBL; AFBP01000014; EGG56797.1; -; Genomic_DNA.
DR RefSeq; WP_008863707.1; NZ_GL883687.1.
DR AlphaFoldDB; F3QII0; -.
DR GeneID; 43348218; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_3_4; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000005156; 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; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR006311; TAT_signal.
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 Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
FT DOMAIN 311..466
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 197..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 476 AA; 53103 MW; FB1849B32C100FED CRC64;
MNTRRSFLEG AGGALLLSFV PWSPAYGAQV VDVRVWPAEE YTRITIEHDA PMKFKYFVLR
NSDPVRLAVD IDGLLLTDKL KQIIQKVKPN DPYISRIRVG QNRPNVVRIS IDFKTDVDPQ
VFSLKPAGQY RYRLVFDIYP ATQKDPLMAI IQKEESEPDA IKSLLAQVAE GQKRMEENRA
DSGEVDQLGQ ILAGIADGSL APMRPDEEPK GSSKPAQKKP AQKKPETQLA QTKPSKTKPA
RSPRVRTLVI MIDPGHGGED PGAIGRRHRT REKDVVLAVA RILRQELNEI EGVKALLTRD
GDYFVPLQRR VQKARAAKAD FFVSIHADAW VKPTARGSSL YVLNTRGQVS TANRWLARKQ
NDADLIGGVN LSNKDKQIAR ILMDMSMTSQ VSDSMVYGAR ILNELSRINQ LHRGKVEQAN
FAVLKAPDIP SVLVETAFLS HPEEEKKLRT RAFQRKLACA IGNGILKGFG HKSRLG
//
