ID W3TYD1_BARQI Unreviewed; 319 AA.
AC W3TYD1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, 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=Q649_01278 {ECO:0000313|EMBL:ETS16312.1};
OS Bartonella quintana JK 73.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=1402976 {ECO:0000313|EMBL:ETS16312.1, ECO:0000313|Proteomes:UP000018945};
RN [1] {ECO:0000313|EMBL:ETS16312.1, ECO:0000313|Proteomes:UP000018945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JK 73 {ECO:0000313|EMBL:ETS16312.1,
RC ECO:0000313|Proteomes:UP000018945};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Kirby J., Birtles R., Dasch G., Hendrix L., Koehler J.,
RA Kosoy M., Young S., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J.,
RA McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A.,
RA Saif S., Shea T., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bartonella quintana JK 73.";
RL Submitted (DEC-2013) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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:ETS16312.1}.
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DR EMBL; AZZX01000009; ETS16312.1; -; Genomic_DNA.
DR RefSeq; WP_011179683.1; NZ_KI911825.1.
DR AlphaFoldDB; W3TYD1; -.
DR PATRIC; fig|1402976.3.peg.1546; -.
DR HOGENOM; CLU_049290_2_0_5; -.
DR Proteomes; UP000018945; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 2.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 7..216
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 319 AA; 35809 MW; 1E44579400911C52 CRC64;
MYQIDYNSYR SVKSFNRRIR FLVMHYTAIN FKESIAALTG MQVSAHYLVP DPLEQTYIEA
GFKDMRIFNL VDENERAWHA GVSSWAGRNN LNDTSIGIEI VNLATSHSDC SEETDAEVAL
KDVRFSNPIH ESGGALQANI GSLAKGNNMG GTALPYHAVN LVPCNNEVFT FPPYNPTQID
AVKELALNVL QRYPDIMPTD VVGHSDIAIG RKSDPGAAFP WKELYVAGIG AWYDDELKEH
YQRQFCESFP SKADIVTKLR CYGYDTSAAG SEIGYNELIR AFQLHFRQEN YDGILDVETA
AIIYALVDKY FPSNEFNVT
//
