ID A0A0B5CG45_NEIEG Unreviewed; 435 AA.
AC A0A0B5CG45;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, 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 Name=amiC {ECO:0000313|EMBL:AJE17978.1};
GN ORFNames=NELON_03180 {ECO:0000313|EMBL:AJE17978.1};
OS Neisseria elongata subsp. glycolytica ATCC 29315.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=546263 {ECO:0000313|EMBL:AJE17978.1, ECO:0000313|Proteomes:UP000031392};
RN [1] {ECO:0000313|Proteomes:UP000031392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|Proteomes:UP000031392};
RA Veyrier F.J., Taha M.-K.;
RT "Complete Genome sequence of Neisseria elongata subsp. glycolytica.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJE17978.1, ECO:0000313|Proteomes:UP000031392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29315 {ECO:0000313|EMBL:AJE17978.1,
RC ECO:0000313|Proteomes:UP000031392};
RX PubMed=26162030;
RA Veyrier F.J., Biais N., Morales P., Belkacem N., Guilhen C., Ranjeva S.,
RA Sismeiro O., Pehau-Arnaudet G., Rocha E.P., Werts C., Taha M.K.,
RA Boneca I.G.;
RT "Common Cell Shape Evolution of Two Nasopharyngeal Pathogens.";
RL PLoS Genet. 11:E1005338-E1005338(2015).
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};
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DR EMBL; CP007726; AJE17978.1; -; Genomic_DNA.
DR RefSeq; WP_041961304.1; NZ_CP007726.1.
DR AlphaFoldDB; A0A0B5CG45; -.
DR KEGG; nel:NELON_03180; -.
DR PATRIC; fig|546263.7.peg.669; -.
DR HOGENOM; CLU_014322_2_2_4; -.
DR Proteomes; UP000031392; Chromosome.
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; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR006311; TAT_signal.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000031392};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..435
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002114537"
FT DOMAIN 270..424
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 163..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..196
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 47371 MW; C203FB7B40ADF7A3 CRC64;
MDKKFTRRQI VRSAAAGLLF TVTPAAFAKA APQFVAVRIW PANAYSRITL ESTEKLQYNY
FTLDNPRRLV LDLKGVQLNE VLQSINSKVQ RSDPYIGIIR VGQNTADTVR IVIDLKTDVN
PQLFTLAPVA NFKHRLVADL YPMHAQDAND PLMALLEDYS KGKISNQGTG SGTPPVQPPP
EVSKPPKTTK TPDDTPPPPP TDRKHHRQPI IVLDPGHGGE DPGAIGKSGL REKDVVLSIA
RETKKRMEGM GYKVYMTRNE DVFIPLGVRV AKARKLNADL FISIHADAFT SPSARGTGVY
TLSTKGASSA AAKFLAQTQN NADAIGGVKT GGNKDIDSTI LDMTQTVTNK DSAILGKKVL
NELGKYNKLH KGDIDQANFA VLRAPDIPSI LVETAFLSNP EEERKLSGMV FRHQCADAIT
AGVRSYLAGA VLARR
//