ID A0A0P9F1R4_9CHLR Unreviewed; 338 AA.
AC A0A0P9F1R4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE Flags: Fragment;
GN ORFNames=SE17_27580 {ECO:0000313|EMBL:KPV50327.1};
OS Kouleothrix aurantiaca.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Roseiflexineae;
OC Roseiflexaceae; Kouleothrix.
OX NCBI_TaxID=186479 {ECO:0000313|EMBL:KPV50327.1, ECO:0000313|Proteomes:UP000050509};
RN [1] {ECO:0000313|EMBL:KPV50327.1, ECO:0000313|Proteomes:UP000050509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COM-B {ECO:0000313|EMBL:KPV50327.1,
RC ECO:0000313|Proteomes:UP000050509};
RA Hemp J.;
RT "Draft genome sequence of Kouleothrix aurantiaca JCM 19913.";
RL Submitted (SEP-2015) 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:KPV50327.1}.
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DR EMBL; LJCR01001455; KPV50327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P9F1R4; -.
DR PATRIC; fig|186479.3.peg.1855; -.
DR Proteomes; UP000050509; 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 Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
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; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000050509}.
FT DOMAIN 197..326
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPV50327.1"
SQ SEQUENCE 338 AA; 36543 MW; 9D77213ACAE08E06 CRC64;
GGATFHPDWA FHQFALASKL GPPLGESATI TIDGAQYAFQ PFALDTLYNK VPNWSDVRRL
SQLANSADAP SVRLRDTLLT QTYARGAAIY HPDWAFHQLA RTWNLGAALS DSYRVASGSA
QYAIQVYATD TLYNVIPNWA DVRRLSQLAN APRPAVLSAR EAPAAAPAPK LPASAQLEPA
PAAFHIVQYS SPQALAVAFG DRSGSKINLL VLHSAPGPVA QILADMTALD TQGMSHYVVA
ADGAIYQLVS DDCAAWHAGM ADWNGRRQNI NRISLGITAE QAGNYPAAQL AALAWLANTL
RARYELPADA VLRWSDLAPD KPSDPDAFPW EAFRKRMK
//
