ID B6AP49_9BACT Unreviewed; 437 AA.
AC B6AP49;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EDZ38844.1};
GN ORFNames=CGL2_11276011 {ECO:0000313|EMBL:EDZ38844.1};
OS Leptospirillum sp. Group II '5-way CG'.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Leptospirillum.
OX NCBI_TaxID=419541 {ECO:0000313|EMBL:EDZ38844.1};
RN [1] {ECO:0000313|EMBL:EDZ38844.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14961025; DOI=10.1038/nature02340;
RA Tyson G.W., Chapman J., Hugenholtz P., Allen E.E., Ram R.J.,
RA Richardson P.M., Solovyev V.V., Rubin E.M., Rokhsar D.S., Banfield J.F.;
RT "Community structure and metabolism through reconstruction of microbial
RT genomes from the environment.";
RL Nature 428:37-43(2004).
RN [2] {ECO:0000313|EMBL:EDZ38844.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=18651792; DOI=10.1371/journal.pbio.0060177;
RA Simmons S.L., Dibartolo G., Denef V.J., Goltsman D.S., Thelen M.P.,
RA Banfield J.F.;
RT "Population genomic analysis of strain variation in Leptospirillum group II
RT bacteria involved in acid mine drainage formation.";
RL PLoS Biol. 6:E177-E177(2008).
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; DS995260; EDZ38844.1; -; Genomic_DNA.
DR AlphaFoldDB; B6AP49; -.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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: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 262..414
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 142..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 48698 MW; B807E6D9BACFA2F7 CRC64;
MKTGFWIAIA TFLFLSGGFG TPSSVFAQNR IGFIKNIRVG LHANRIRIVA VLDRLPKDPP
VYTPGPRGSL SFPGLMPSPS IHKRVIAHSG ALKAHFREIN IEYAPGHQET RLTIIGPISE
STPHFFTLHH PDRIVADFPF SAQTSSRKTS PSQKANAVPP RPGQKVIVIP GKKVSETHMA
RALPAAFSPS APLPVRAPRF RVVIDPGHGG KDCGTLGVNG VCEKDLVLDI ALDLRKRLES
DRRFRVLMTR DQDIFIPLKE RTDMANRWKG DLFLSIHANS DPNRAVRGIE TFLLNLRSSD
KRSKEVAMRE NTVLGVSHGD LGAILLTLRV NHKKKRSLEF AGDLDRSFSR NLEGQYQGVR
NLGIRQAPFY VIMGTSMPAA LTEINFLSNP DDARIMASRT YRKLVARALY RGIVQYYRRV
HPEIQAENNR SPLLAHP
//