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Database: UniProt
Entry: B6AP49_9BACT
LinkDB: B6AP49_9BACT
Original site: B6AP49_9BACT 
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).
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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
//
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