ID A0A0A1MKI1_9BACI Unreviewed; 425 AA.
AC A0A0A1MKI1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase LytC {ECO:0000313|EMBL:CEI83613.1};
GN Name=lytC {ECO:0000313|EMBL:CEI83613.1};
GN ORFNames=BN997_03530 {ECO:0000313|EMBL:CEI83613.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI83613.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI83613.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI83613.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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DR EMBL; CDGG01000001; CEI83613.1; -; Genomic_DNA.
DR RefSeq; WP_052485062.1; NZ_JAUDBP010000016.1.
DR AlphaFoldDB; A0A0A1MKI1; -.
DR STRING; 545501.BN997_03530; -.
DR Proteomes; UP000040453; Unassembled WGS sequence.
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; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR003646; SH3-like_bac-type.
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 Pfam; PF08239; SH3_3; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000040453};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..425
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001986284"
FT DOMAIN 27..89
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
FT DOMAIN 127..188
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
FT DOMAIN 312..421
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 93..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 47196 MW; 94F4EEA4DC47F0D1 CRC64;
MKYNLMIGIA FLICLFIFIP TVHADNGTLY KVDTETTELM DAPAQDTVLL SELKKDYKVT
IFEESNGWGK TFYNGEQAWV ALHHLSAVDE IQTEPENEQS DTEDNQAETA AAAAETNTET
AEPAENGQLY RIQAPAVNVR NAPDKNAAVV TQMNHGEKVT IFEELYGWGK TYYHDEEVWI
TLYLLDKDDE SNGNSDTSEE NEKTESLETV EETENEASEA TSEPKDGESE KENGETKEVQ
AEQSTENPLA GRQFVIDPGH GGKDPGAVGS EAHEKTLALT TAKKLGEQLR HQGASVTFTR
EDDTYLSLGE RVNISNSANP DAFISLHYNA SEDQAAHGVE TFYKNESESQ MLAEYVQTSL
MSHVHLDNRG AKQADFQVLR ENQQTAILIE LGFISNSEEQ QTIQTDNYQN HAAEGIIAGL
EDYFS
//
