ID   A0A143DFR1_9PROT        Unreviewed;       416 AA.
AC   A0A143DFR1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=AY555_06225 {ECO:0000313|EMBL:AMW35592.1};
OS   Haematospirillum jordaniae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Novispirillaceae; Haematospirillum.
OX   NCBI_TaxID=1549855 {ECO:0000313|EMBL:AMW35592.1, ECO:0000313|Proteomes:UP000076066};
RN   [1] {ECO:0000313|EMBL:AMW35592.1, ECO:0000313|Proteomes:UP000076066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H5569 {ECO:0000313|EMBL:AMW35592.1,
RC   ECO:0000313|Proteomes:UP000076066};
RA   Nicholson A.C., Humrighouse B.W., Loparov V., McQuiston J.R.;
RT   "Complete Genome of H5569, the type strain of the newly described species
RT   Haematospirillium jordaniae.";
RL   Submitted (FEB-2016) 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};
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DR   EMBL; CP014525; AMW35592.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143DFR1; -.
DR   STRING; 1549855.AY555_06225; -.
DR   KEGG; hjo:AY555_06225; -.
DR   Proteomes; UP000076066; 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   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.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000076066}.
FT   DOMAIN          250..404
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          139..184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   416 AA;  45117 MW;  9562DB55F545AB36 CRC64;
     MLAGAAGLAG VVLFSSHGAE AVGARNVRLG NHGTFTRVVI DVTGDVPFSA FSLTNPARII
     IDLPEIDWQF EQPAVPGKPG LLVKAMRYGL FQPGNSRIVL DLAEPAAVKN MFVLPPGEQT
     SWRLVVDLAP VDAAMFQRSA GPGNRTGTFR PKHGPQDTEP ATTQVDNTLP RQPMTPEKRK
     AVPSPAKPVI VLDPGHGGID PGATGVSGIF EKNLTLSTAR ELKAALDKTG RYTVHLTRDR
     DIFLQLRERV AIARTHRADL FISIHADAGA KPSIRGLSVY TLSDNASDAE AAALATSENK
     ADIIAGIDLS HESKEVTNIL IDLAQRETMN LSSRLAEIVI AELRRDITLL PRSHRFAGFA
     VLKAPDIPSF LMEMGYLTNR DEERLLRTRG YRKKLASAMV RAIDRYFSAT QKASLP
//