ID A0A0B7I956_9FLAO Unreviewed; 398 AA.
AC A0A0B7I956;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:CEN46597.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:CEN46597.1};
GN ORFNames=CCAND38_370029 {ECO:0000313|EMBL:CEN46597.1}, CKY20_06505
GN {ECO:0000313|EMBL:RIY36585.1};
OS Capnocytophaga canis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1848903 {ECO:0000313|EMBL:CEN46597.1, ECO:0000313|Proteomes:UP000045051};
RN [1] {ECO:0000313|EMBL:CEN46597.1, ECO:0000313|Proteomes:UP000045051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CcD38 {ECO:0000313|EMBL:CEN46597.1,
RC ECO:0000313|Proteomes:UP000045051};
RA Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RIY36585.1, ECO:0000313|Proteomes:UP000265497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-158 {ECO:0000313|EMBL:RIY36585.1,
RC ECO:0000313|Proteomes:UP000265497};
RA Gulvik C.A.;
RT "Capnocytophaga canis 17-158 assembly.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CDOI01000148; CEN46597.1; -; Genomic_DNA.
DR EMBL; NSDI01000005; RIY36585.1; -; Genomic_DNA.
DR RefSeq; WP_042344367.1; NZ_WLVI01000013.1.
DR AlphaFoldDB; A0A0B7I956; -.
DR Proteomes; UP000045051; Unassembled WGS sequence.
DR Proteomes; UP000265497; 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; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:CEN46597.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000045051};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..398
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033715202"
FT DOMAIN 86..243
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 265..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 44280 MW; FF94AB3AB617C892 CRC64;
MKNILLFLAL LVSNLIFSQK TPTFNVVLDA GHGGKDPGKI GKGKIYEKDV ALNIVLEVGK
ILEQHSDIQV IYTRKKDVFV DLYERGAIAN RAKADLFVSV HCNAHHTQAA GSETFVLGLS
ANDRNMEVAK TENAVIYLED NYKTKYAAYN INSPESFIGL SIMQEEFLEQ SIQLAKYVQD
NFTNVMQRNN RGVKQAPFIV LHQTYMPSIL VETGFLSNND ELKFLASKKG QTDFAENIAD
AILSYKTWVQ SRSSHIVPEN FIEETPAKSS EKKASSPKKT NNIKKTAKTT SKSSNTTKKN
NSTTQKKGNI KKSKVVYKIQ LSSSAKKIEA KPYNFKKLSP ISSVKCGNLY CYLYGAASKR
SEANVLLANA KKVGYKDAYI IAYLDGKPVQ LSVAEKNE
//
