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Database: UniProt
Entry: B2HML0_MYCMM
LinkDB: B2HML0_MYCMM
Original site: B2HML0_MYCMM 
ID   B2HML0_MYCMM            Unreviewed;       550 AA.
AC   B2HML0;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   SubName: Full=Conserved hypothetical secreted protein {ECO:0000313|EMBL:ACC43779.1};
GN   OrderedLocusNames=MMAR_5375 {ECO:0000313|EMBL:ACC43779.1};
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=216594 {ECO:0000313|EMBL:ACC43779.1, ECO:0000313|Proteomes:UP000001190};
RN   [1] {ECO:0000313|EMBL:ACC43779.1, ECO:0000313|Proteomes:UP000001190}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M {ECO:0000313|Proteomes:UP000001190};
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
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DR   EMBL; CP000854; ACC43779.1; -; Genomic_DNA.
DR   AlphaFoldDB; B2HML0; -.
DR   STRING; 216594.MMAR_5375; -.
DR   KEGG; mmi:MMAR_5375; -.
DR   eggNOG; COG5479; Bacteria.
DR   HOGENOM; CLU_018529_1_1_11; -.
DR   OMA; IGDAWAQ; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR013207; LGFP.
DR   InterPro; IPR015510; PGRP.
DR   InterPro; IPR006619; PGRP_domain_met/bac.
DR   PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN RECOGNITION PROTEIN 5; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF08310; LGFP; 1.
DR   SMART; SM00701; PGRP; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001190}.
FT   DOMAIN          206..354
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   REGION          103..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   550 AA;  58435 MW;  56EF2EA06007287A CRC64;
     MPSRSRAPTM LLTAIAATVV IVSWVLTRPP PSTHEQPSAQ DTRLVEQPLV GLGGGVTVRQ
     LTQDEPFSLV ALTGDLVGTS ARMRARQSDG SWGPWYQAEY ETAAPDEQGA GAPATAGTSE
     RPRSTEPVFV GTTNTVEIAV TRPIDAPVTQ PPPTGEPEPV DLGYRPATKE LPFGQNISAV
     LISPPQAPAG THWTPPTGVT MPGQAPPIIS RADWGADEAL RCESPEYDRA VRAAVVHHTA
     GSNDYSPLES AGIVKAIYTY HSKTLGWCDI AYNALVDKYG QIFEGSAGGL TKPVEGFHTG
     GFNRDTWGVA MIGNFDDVAP TPLQIRAVGR LLGWRLGIAE VDPKSMVELE STGSSYTTVP
     GGAIAKLPAI FTHRDVGNTD CPGNAAYALM DEIREIASHF NDPPEELLKS LEGGAIYQRW
     QELGAMNSVL GAPTSPEADG ADGARYATFA KGAMYWSPTT GAQPVTGAIY DAWASLSYER
     GPLGLPTSAE IQEPLRITQN FQHGVLNFQR LTGNVSEVVN GITTPLATKP PSGPMVPPEH
     FSLPIHPIIP
//
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