ID A0A286GR90_9PROT Unreviewed; 423 AA.
AC A0A286GR90;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SAMN05421508_107167 {ECO:0000313|EMBL:SOD98040.1};
OS Caenispirillum bisanense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Novispirillaceae; Caenispirillum.
OX NCBI_TaxID=414052 {ECO:0000313|EMBL:SOD98040.1, ECO:0000313|Proteomes:UP000219621};
RN [1] {ECO:0000313|EMBL:SOD98040.1, ECO:0000313|Proteomes:UP000219621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=USBA 140 {ECO:0000313|EMBL:SOD98040.1,
RC ECO:0000313|Proteomes:UP000219621};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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 ---------------------------------------------------------------------------
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; OCNJ01000007; SOD98040.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286GR90; -.
DR Proteomes; UP000219621; 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; 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:UP000219621};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..423
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012176916"
FT DOMAIN 257..411
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 160..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 46389 MW; 00E7362476766ACB CRC64;
MAAWPFPTVT RRMVMLGAAA TAALGGVLRP SEAWAAVRAS AVRLGNHQEF TRFVLDVSQA
IDFSLFTLTE PNRIVLDLPE VEWSFGEENL PPAKGVVSAL RWGLFQPGQS RVVLDLVRPA
TVKQAFLLPP NGQAGWRFVL DLQETTAAQF LAAAGPERRI GSLKTAPEPT GGVQEAALRP
APQATQPPRD PNRPKVIVLD PGHGGVDPGA IGASGVYEKN ITLAAAREFR DILQKSGRFK
VVLTRDRDIF LPLRDRFEVA RRHDADLFIS LHADSIKNPA VRGLSVYTLS EKASDSEAAA
LADKENKADI IAGIDLSHES VEVTNILIDL AQRETMNLSS RIAEQLIDEL QRDVKLLRQS
HRFAGFAVLK APDVPSILVE MGYLSNADEE RLLRQAAYRA KLGKALERTL DGFFSRTQKA
YRP
//
