ID M1QH88_BACTU Unreviewed; 579 AA.
AC M1QH88;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:AGG04062.1};
GN ORFNames=H175_ch5353 {ECO:0000313|EMBL:AGG04062.1};
OS Bacillus thuringiensis serovar thuringiensis str. IS5056.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1286404 {ECO:0000313|EMBL:AGG04062.1, ECO:0000313|Proteomes:UP000011719};
RN [1] {ECO:0000313|EMBL:AGG04062.1, ECO:0000313|Proteomes:UP000011719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IS5056 {ECO:0000313|EMBL:AGG04062.1};
RX PubMed=23516221;
RA Murawska E., Fiedoruk K., Bideshi D.K., Swiecicka I.;
RT "Complete genome sequence of Bacillus thuringiensis subsp. thuringiensis
RT strain IS5056, an isolate highly toxic to Trichoplusia ni.";
RL Genome Announc. 1:E0010813-E0010813(2013).
CC -!- SIMILARITY: Belongs to the peptidase C40 family.
CC {ECO:0000256|ARBA:ARBA00007074}.
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; CP004123; AGG04062.1; -; Genomic_DNA.
DR RefSeq; WP_000760274.1; NC_020376.1.
DR AlphaFoldDB; M1QH88; -.
DR SMR; M1QH88; -.
DR GeneID; 67469368; -.
DR KEGG; btht:H175_ch5353; -.
DR PATRIC; fig|1286404.3.peg.5388; -.
DR HOGENOM; CLU_016043_13_5_9; -.
DR Proteomes; UP000011719; Chromosome.
DR Gene3D; 3.90.1720.10; endopeptidase domain like (from Nostoc punctiforme); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 5.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR34408; FAMILY PROTEIN, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR34408:SF1; GLYCOSYL HYDROLASE FAMILY 19 DOMAIN-CONTAINING PROTEIN HI_1415; 1.
DR Pfam; PF00877; NLPC_P60; 1.
DR Pfam; PF08239; SH3_3; 5.
DR SMART; SM00287; SH3b; 5.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
DR PROSITE; PS51781; SH3B; 5.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..579
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038943908"
FT DOMAIN 46..108
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 117..179
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 200..262
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 285..347
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 367..429
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 459..579
FT /note="NlpC/P60"
FT /evidence="ECO:0000259|PROSITE:PS51935"
FT REGION 180..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 61105 MW; B7B4EB2C9E8522BE CRC64;
MKKYLAGLAA VSVAGGAAPT LDSVQAAPEQ NTQKAATTVQ ASASNNSSYT VNASVLHVRA
GSSTSHDIIS RVYNGQSLNV IGEENGWFKI NINGKTGFVS GEFVSKSGAA NNNVSTGGNN
KVTADVLRVR TAPNTSSSVS GRVYEGQTLN VIGQENGWVK INHNGQVGYV SGEFVSGVSS
NAGSSNNNTN NNNQEVKPAS GNYTVNVSSL RVRTGPSTSH TTVGSVKKGQ VVQVVGEVQD
WFKINYAGQT AYISKDYVTK GGSNENVTEG NKQEQNNNNG TIQTGGSYVV NATSLRVRTG
PAAYHSVIGG VLNGTTLNVV GSENGWFKVN YQGKTGFVSS EFVKFVKGGT TTPEQPKQPE
KPNQGAIGDY YINASALNVR SGEGTNYRII GALPQGQKVQ VISENSGWSK INYNGQNGYI
GTRYLSKTPV GGAVDNKPNN NQNNNQNNNN NNNNTGNNSG DSSSVLAYAK SMQGVPYVWG
GTSANGVDCS GYIYHVFKKF GHNISRQSVA GYWSSLPQTS NPQPGDLIYF QNTYKSGPSH
MGIYLGGGSF IQAGDKGVAI ASLSNSYWKS HFLGYTKAP
//
