ID L0J5W5_9MYCO Unreviewed; 2085 AA.
AC L0J5W5;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Metalloendopeptidase-like membrane protein {ECO:0000313|EMBL:AGB26684.1};
GN ORFNames=Mycsm_06547 {ECO:0000313|EMBL:AGB26684.1};
OS Mycobacterium sp. JS623.
OG Plasmid pMYCSM01 {ECO:0000313|EMBL:AGB26684.1,
OG ECO:0000313|Proteomes:UP000010844}.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=212767 {ECO:0000313|EMBL:AGB26684.1, ECO:0000313|Proteomes:UP000010844};
RN [1] {ECO:0000313|EMBL:AGB26684.1, ECO:0000313|Proteomes:UP000010844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS623 {ECO:0000313|EMBL:AGB26684.1,
RC ECO:0000313|Proteomes:UP000010844};
RC PLASMID=pMYCSM01 {ECO:0000313|EMBL:AGB26684.1,
RC ECO:0000313|Proteomes:UP000010844};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Mattes T., Holmes A., Rutledge P.,
RA Paulsen I., Coleman N., Woyke T.;
RT "Complete sequence of plasmid 1 of Mycobacterium smegmatis JS623.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003079; AGB26684.1; -; Genomic_DNA.
DR KEGG; msa:Mycsm_06547; -.
DR PATRIC; fig|710686.3.peg.6589; -.
DR HOGENOM; CLU_232600_0_0_11; -.
DR Proteomes; UP000010844; Plasmid pMYCSM01.
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; cd12797; M23_peptidase; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 2.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR025442; DUF4185.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR016047; Peptidase_M23.
DR InterPro; IPR015020; Rv2525c-like_Glyco_Hydro-like.
DR PANTHER; PTHR48125; LP07818P1; 1.
DR PANTHER; PTHR48125:SF10; RNA POLYMERASE II-ASSOCIATED FACTOR 1 HOMOLOG; 1.
DR Pfam; PF01510; Amidase_2; 2.
DR Pfam; PF13810; DUF4185; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR Pfam; PF08924; Rv2525c_GlyHyd-like; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 2.
PE 4: Predicted;
KW Plasmid {ECO:0000313|EMBL:AGB26684.1}.
FT DOMAIN 346..446
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT DOMAIN 512..683
FT /note="Rv2525c-like glycoside hydrolase-like"
FT /evidence="ECO:0000259|Pfam:PF08924"
FT DOMAIN 1107..1221
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|Pfam:PF01510"
FT DOMAIN 1450..1564
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|Pfam:PF01510"
FT DOMAIN 1746..2064
FT /note="DUF4185"
FT /evidence="ECO:0000259|Pfam:PF13810"
FT REGION 460..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1078
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1424
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2085 AA; 226169 MW; AD644C1E3D7BB358 CRC64;
MAAHTTATFA RPQAKRIERL GKKIFKECIA GDDSLLTPGV QVWTQDNLAE LHRRVIDASD
AARGTISDRA DAALADASNQ VRQLFAEICI LHQLPLSNTV AKRAAKVRLI KEILRPIEPP
VALPADIDEA FADGMVDVSR SAGSRRWAQL GVIVAFAEYF KAQELRIRHR AASDPATLRQ
LMLAAPSDPE PAQRQALLYL LKPDYFLPIV GRRNRARLRD ALAAEYLPGG ASQDLDADLR
AIDDAVQAEA GGPVDYYVAP WRERWLQDGS APTPTNGEVA QNGNGHAAVG ADAIGIAADA
MPAAVDAPPA PPTPPAPPAP RRKYLPMVPG TYRQSSGFRP PDRPDHNGID FAADLGTPIY
AVSDGFLAHV GINDDPTGFG SWLVLDAQEQ WHLDFVFGHM PPSSFINPDT GARWQEGDRV
RAGQQIAVVG SEGGSTGPHL HFETWSPPGR FGGQVLDPAQ SWLPDATDPR QAEADRAAAT
SAPATPVPPA PARSLVGAML VDYSAGVPSA TAIAAQGFVG AVRYVSDRRA DWMVGKPLTK
AEADDLRSHG LAVVSNFQFG KRDWDGGAEQ GRTDAQRGMQ LHHDAGGPDD AVIYVSVDAD
PTDDEWNTKV VPYLQAWQER LGKQRMGIYC NAPCIDRAQR DGLGSYFWQH NWGSAGRIHP
DAHIHQFEID QQSVGGIGVD RNHILKEDFG QWDRGAAAGA PIAQPGADKF PLPPGFYWGP
LDGPEESWSN SAGTEPQYSK DGLRRWQQTL GLPATGVFDD VTKAAGLKIQ RAMGWSPNGS
VHEAEWNAVI RDGWRPPAGE PWPPAPALST KDSYAQAIIA EGIRRHVTPR GIKIALSTAL
VETNMRIYAN SKDQASLLLP HDAVGSDGMS VGLFQQQNFA EWKSLECRMD AACSAGTFYE
HLEQLDYNNE AMSPGSFAQA VQRSKFPTRY DDRFSEASAL YDRLAATVDA QPDPTPVDAN
RYPLPPGIYW GPLEGPDESW SNIAGTEPQY SKDGLRRWQE SVGIKGTGIY DDATRNAAVQ
MQQHFGTART GTVGADEWDE VILKGWHLPA GDGQATPTPT QTPTPTPAPT PTPAPQPAGG
VKSPGGYPIT RVDGPGFNRG HGDYLRIYLH TTESQDWITT ADNVAAYQAR QQDGSYHYLV
DDSHIINTVA TTDTAWGVLS DNGVSVQIAM VGTSGEIERW QGDNPNSENR PKSREQWLAH
DTMLDMVAYM IAIVSRDHSI PIERVDIDGV GANRRGVSSH NNYTYGSVKL KGFKDGTHWD
VPDTFPYDVV LAAAKGYERI VNDPDRFPLP AGIYWGPLDG PDESWSNQGG TEPQASIDGL
RRWQLAVGVP GSGIYDDATR DAALQMQAQF NWTPTGTIDG NEWDQVIRKG WHLGAAQPKP
QPVAQPLPVA PPQPAPTPVT PAVAVAPPPP PPPPPQPVQP QPTVKSPGGY PITWVAGPGY
NQGHNEYVRI YLHTTENQDF VSTAEAVAAY QAQKQDGSYH YIVDDNHIIN TVATKNTAWG
VLSDNAFTVQ IAMVATSGEI GQWQGDNPNR EERPKSREQW LAHDTMLDMV AYMIAIVSRD
HSIPIERVDI DGVGANRRGV SSHNNYTYGS VKLKGFKDGT HWDVPDTFPY DVVLAAAKAY
LATITDPDTF PLPQGHYWGP LDGPEESWSN MFGNEPQSSK DGLKRWQLAL GIPGSAIYDD
ATKDAATQMQ HAMGWPQTGT VGEAEWNEVI KRAWRLPPPT PPAPIPAIDP GPAVGSSKKI
KDATGPGLTD QFGMAATDLG VMTRTPSGRI LAVFGDTFRG PRVGDGDWRA PVGLFSDTKK
LDDGIVWSEA SGGVAGYAAQ LWPYPHDNPV FSTVLPSDVI TVGDTIYLHA MVNEGLGNVV
WTEIWKSTDD GHTWQHSGAK FDAGLHNGLA QMWTWDLCED GWVYILSTGF QRDKPLILRR
VQPTGITDPS AYQTWGVTDG VGGWGNAPTP VLQGAGQDDK FGELCLRRID NQWVLVDFDS
SDAGGYDIDV RVFTDITGNL NDAHISTPIR GVGWGQEGDD AVAQLYGPSI VPGSTLNGGF
HILLSQWKTD GPDKGWPYRA MQFKIPVTCD AGFRDDGAVN PHGGR
//
