ID AMIB_BUCAI Reviewed; 237 AA. AC P57638; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Putative N-acetylmuramoyl-L-alanine amidase; DE EC=3.5.1.28; GN Name=amiB; OrderedLocusNames=BU576; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). CC -!- FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell CC division. {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family. CC {ECO:0000305}. 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; BA000003; BAB13265.1; -; Genomic_DNA. DR RefSeq; NP_240379.1; NC_002528.1. DR RefSeq; WP_009874524.1; NC_002528.1. DR AlphaFoldDB; P57638; -. DR SMR; P57638; -. DR EnsemblBacteria; BAB13265; BAB13265; BAB13265. DR KEGG; buc:BU576; -. DR PATRIC; fig|107806.10.peg.580; -. DR eggNOG; COG0860; Bacteria. DR HOGENOM; CLU_014322_4_1_6; -. DR Proteomes; UP000001806; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. 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:SF6; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIB; 1. DR Pfam; PF01520; Amidase_3; 1. DR SMART; SM00646; Ami_3; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. PE 3: Inferred from homology; KW Cell wall biogenesis/degradation; Hydrolase; Reference proteome; Secreted. FT CHAIN 1..237 FT /note="Putative N-acetylmuramoyl-L-alanine amidase" FT /id="PRO_0000164421" FT DOMAIN 7..225 FT /note="MurNAc-LAA" FT /evidence="ECO:0000255" SQ SEQUENCE 237 AA; 27240 MW; D8FD528FB89C406C CRC64; MSKKITILID AGHGGYDPGA IGIRGLKEKN INIEIALKLE KLLNHDKMFC TILTRHNDSY LSLKKRKQLL KKNQVNFLIS IHADSSRKQN VSGASIWIVS KTRINREINN YLKNKSTLLF SKKIENIFKQ NKNDFFLKKT ILDLQSNNFQ KIELDLSKEI LKQLEKNTKL NKKYPNYASL GILSSINTPS ILIETGFITN ILEGKKLKTT NYQNKIANSI YLGLKNYFTK SSYILKK //