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Database: UniProt
Entry: A0A2B8AZX6_9PROT
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Original site: A0A2B8AZX6_9PROT 
ID   A0A2B8AZX6_9PROT        Unreviewed;       496 AA.
AC   A0A2B8AZX6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=CRT60_32585 {ECO:0000313|EMBL:PGH54514.1};
OS   Azospirillum palustre.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=2044885 {ECO:0000313|EMBL:PGH54514.1, ECO:0000313|Proteomes:UP000225379};
RN   [1] {ECO:0000313|Proteomes:UP000225379}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2 {ECO:0000313|Proteomes:UP000225379};
RA   Kravchenko I.K., Grouzdev D.S.;
RL   Submitted (OCT-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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PGH54514.1}.
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DR   EMBL; PDKW01000043; PGH54514.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B8AZX6; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000225379; 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; 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;
FT   DOMAIN          329..484
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  52612 MW;  6B66D6E87EE83480 CRC64;
     MPRPPSLPAA PDRHPHSARS PRRSVGRVLG VLVLALVLLG FGSAGMTAGT ATAQTTAALP
     AALPRTAVVD ARLGIHPDKT RFVLELSDPV SFTVSVAADP YRIVVDLPDL IWPGGALPVE
     GKGVVARYHH TGGPRGTRLT FETVGPARLR EGYMIPARDG HQPRLVLDLE KTTPAEFRQL
     AVAGRDAREV GGKGQLTMSS IVSSAMAVPA PVPASQPSPP ADPASTVPAP PPFAPLPPIP
     PAQLIPAALP VAPPLPDNKP PTVAEKPLIV LDPGHGGQDP GAIGVGGIYE KDITLATARE
     VKRQLEATGR YRVKLTRDSD VFIRLRDRVA IGREAGADLF ISLHADSISS GDMRGLSIYT
     LSDKASDREA EMLAAKENKA DALVGLDLSG ENQLVANILI DLAQRDTMNH SKRFATLALQ
     TLGRDVPLIS SRPHRQAGFA VLTAPDVPSA LIEMGYLSNR QDVGLLTSGA HRERLGKSLA
     RTIDSYFRWL HGSQRS
//
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