ID   A9WEZ3_CHLAA            Unreviewed;       951 AA.
AC   A9WEZ3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   OrderedLocusNames=Caur_2096 {ECO:0000313|EMBL:ABY35308.1};
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602 {ECO:0000313|EMBL:ABY35308.1, ECO:0000313|Proteomes:UP000002008};
RN   [1] {ECO:0000313|Proteomes:UP000002008}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl
RC   {ECO:0000313|Proteomes:UP000002008};
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000909; ABY35308.1; -; Genomic_DNA.
DR   RefSeq; YP_001635697.1; NC_010175.1.
DR   AlphaFoldDB; A9WEZ3; -.
DR   STRING; 324602.Caur_2096; -.
DR   EnsemblBacteria; ABY35308; ABY35308; Caur_2096.
DR   KEGG; cau:Caur_2096; -.
DR   PATRIC; fig|324602.8.peg.2377; -.
DR   eggNOG; COG0739; Bacteria.
DR   eggNOG; COG1572; Bacteria.
DR   eggNOG; COG2133; Bacteria.
DR   HOGENOM; CLU_309891_0_0_0; -.
DR   InParanoid; A9WEZ3; -.
DR   Proteomes; UP000002008; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   InterPro; IPR015510; PGRP.
DR   InterPro; IPR006619; PGRP_domain_met/bac.
DR   PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF07691; PA14; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SMART; SM00758; PA14; 1.
DR   SMART; SM00701; PGRP; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002008};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          702..854
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   951 AA;  104464 MW;  39E568C98F7866FE CRC64;
     MTSWFRLVIC IGILWALMLP WSARSAGLER TVDGRPDEQL FVADQTVAPG DTLPLLPAAD
     GFLTPPTPAP RPFTHMLLRW SAAPDLNPRL ALRVSADGVV WSDWYEVQED DELWQPADGP
     DLHWSEMVYV GADRHWYQVR VDAPSAPSTF RSLLVSTVDS RFGPAAPTAT MSSQPAAVAR
     PPVVSRTAWG NPHGQTSPLA PPAYYPVRHL VIHHTADSNT LAEGQTWADR VRAIWSFHTY
     TRGWGDIGYN YLIDPNGVIY EGRAGGDDVV GFHDTANYGS MGVSLIGTYS SAAPTAAAVD
     SLVALLAWKA DQKRIDPFGR SFYYGCSISR FCSPFNPGAV IDHISGHRQV TPGHTTCPGD
     ALFNLLPQIR QRVQARLAGE SQPDNGDLIV EEHESGFTRS NANWYQMACG YGGTTLYTFA
     TDKQSESTNY ATWRPNLPAS GVYRVLVHVP AGCTALNVSQ QARYRITTAG GVVERVVNQA
     AQTGWIDLGT YNFAASTASL YLSDLTGEPL SGQRAVLFDA VQWQPIDTSR QRMELVAVEY
     GATTIAAGEV LPVRFTVRNV GSDPIYGQDP QGGSVFDLSS DQFEREGYVY DEGECFLGAA
     NQDYPTFPKE AGRFRVMLGP QDRTVTCAGE TGGYPWRWGI SGRLDPGETQ TIVGYVRFRT
     PGVVTLRAGA IHEYVSYVAL AQAEQQITIT PERQSPQVTR YTGLFQPLAM VYELANTPER
     LLARTQNPLS IRRGALLGSF VWYGDLREWG DGGPVPERNN HFLIEQTRTF VAPVSGEYTF
     ELSSDDGAWL WVNERLVVAN TGLHPLRTLS GTITLTAGLH TLSVKYFELD GSAAVGYRVK
     EPGASDFQLV RDGLSSGEIL GSLFRRLDGL RLSASDLGGG STLLRYSWDG ETWVTTTEPF
     IEIGALADGD YHLRYQAFDS NRNESEVVSL QFRVDSNVTV YQVMLPLVTR E
//