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
//