ID   B3PDC4_CELJU            Unreviewed;       462 AA.
AC   B3PDC4;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 83.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase AmiC {ECO:0000256|ARBA:ARBA00074581};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   OrderedLocusNames=CJA_3082 {ECO:0000313|EMBL:ACE84746.1};
OS   Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS   cellulosa).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Cellvibrionales; Cellvibrionaceae; Cellvibrio.
OX   NCBI_TaxID=498211 {ECO:0000313|EMBL:ACE84746.1, ECO:0000313|Proteomes:UP000001036};
RN   [1] {ECO:0000313|EMBL:ACE84746.1, ECO:0000313|Proteomes:UP000001036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ueda107 {ECO:0000313|EMBL:ACE84746.1,
RC   ECO:0000313|Proteomes:UP000001036};
RX   PubMed=18556790; DOI=10.1128/JB.01701-07;
RA   Deboy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA   Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA   Nelson K.E.;
RT   "Insights into plant cell wall degradation from the genome sequence of the
RT   soil bacterium Cellvibrio japonicus.";
RL   J. Bacteriol. 190:5455-5463(2008).
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: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000256|ARBA:ARBA00010860}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00257}.
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; CP000934; ACE84746.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3PDC4; -.
DR   STRING; 498211.CJA_3082; -.
DR   KEGG; cja:CJA_3082; -.
DR   eggNOG; COG0860; Bacteria.
DR   eggNOG; COG1388; Bacteria.
DR   HOGENOM; CLU_014322_2_3_6; -.
DR   Proteomes; UP000001036; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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; cd00118; LysM; 1.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   FunFam; 3.40.630.40:FF:000001; N-acetylmuramoyl-L-alanine amidase; 1.
DR   Gene3D; 2.60.40.3500; -; 1.
DR   Gene3D; 3.10.350.10; LysM domain; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR018392; LysM.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR050695; N-acetylmuramoyl_amidase_3.
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   Pfam; PF01476; LysM; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF54106; LysM domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00257};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001036};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transcription {ECO:0000256|PROSITE-ProRule:PRU00257};
KW   Transcription regulation {ECO:0000256|PROSITE-ProRule:PRU00257}.
FT   DOMAIN          414..440
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50943"
FT   DOMAIN          416..459
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
SQ   SEQUENCE   462 AA;  49579 MW;  18E04F10C7DAD77C CRC64;
     MVLLCSSLVE AANINGVRVW RAPDHTRIVF DLDGPVVHTL STASNPERVI LDITNVKLNT
     GTQGLALADT PISQIRSSVQ NQRDLRLVLD LKTRVRPNSF SLKAHGTMHD RLVLDLHDLA
     LTETTAAVAP QPVVPAPVPS LNTPTAQVAK PAPAQPVRPT QEINGKRNIV VAVDAGHGGE
     DPGAIGPNRL REKEVTLAIS RELVAAINAQ PGFSAKLTRT GDYFIPLKKR RDIARTMKAD
     LFVSIHADAF TRASARGASV FALSRTGATS ETARFLAERE NESDLIGGVG SISLDDKDQV
     LAGVLVDLSM TATLNSSLQV GSHVLRSMGG IAHLHKRQVE QAGFMVLKSP DVPSILVETG
     FISNPDEARK LATPAYRKQM ADALFKGIKQ YFMQHPPAGT LLAAQMASGQ VKGIEREHTV
     ASGDTLSAIA MRYGVSVNQL MRHNSMRTTT VKVGQTLKIP AS
//