ID R7ZF20_LYSSH Unreviewed; 639 AA.
AC R7ZF20;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase peptidoglycan hydrolase LytC {ECO:0000313|EMBL:EON72594.1};
GN ORFNames=H131_10653 {ECO:0000313|EMBL:EON72594.1};
OS Lysinibacillus sphaericus OT4b.31.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1285586 {ECO:0000313|EMBL:EON72594.1, ECO:0000313|Proteomes:UP000013911};
RN [1] {ECO:0000313|EMBL:EON72594.1, ECO:0000313|Proteomes:UP000013911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT4b.31 {ECO:0000313|EMBL:EON72594.1,
RC ECO:0000313|Proteomes:UP000013911};
RA Pena-Montenegro T.D., Dussan J.;
RT "Draft genome of the heavy metal tolerant bacterium Lysinibacillus
RT sphaericus strain OT4b.31.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EON72594.1}.
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DR EMBL; AQPX01000017; EON72594.1; -; Genomic_DNA.
DR AlphaFoldDB; R7ZF20; -.
DR PATRIC; fig|1285586.5.peg.2159; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG3103; Bacteria.
DR HOGENOM; CLU_029344_1_0_9; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000013911; 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 InterPro; IPR001119; SLH_dom.
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; 2.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 3.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 2.
DR PROSITE; PS51272; SLH; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EON72594.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..639
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004461607"
FT DOMAIN 27..93
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 154..216
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 228..294
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 388..450
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 639 AA; 70689 MW; 023E77139E175E0D CRC64;
MYLKKISLML CILFISASIF SIHNASASGG FEDISSNHEA YEQINYLVNS GVIKGYTEKG
KIYYKPNNNV TRGQVAKMVV VASGNKPLVV KKSSFSDVTV GTELSGYVES AKQLGFFATN
TKDKFLPNMP LTRDEMSFVL TKAFKLDSSE YEKVDSPFVD VDMTHPYIQY VKTIYYNGIT
KGSGQNYNPN GQVTRAQFAL FVARAKSEKY RLELPVKDVD VPDASQIIGT VQVTTDGLNI
RNTKDSSSKA NIVGTVNKGD KLSVYAAEGD WLKVSSKDAY TYIYKTYAQF LDADGNTLEN
VQKQVTTTQS INVYVKASSS SKIISTVNSK VKLPVYKTVN GYYLTEVGDV PGYIVANSTE
DVTVEQPAIP VPDLKPTPDP ITPPVTGDLL GRVTVDNLNI RKEANSTSMV LGKLSKGEYV
QVNSIYDYWA QVTFEDQTGY VHKSYLKLLN QSGNPLKDRI IIIDPGHGGK DPGTSFESFS
EKNITLKVGT LVKDKLEAAG AKVLMPRTGD TFPTPQDRVD FSHANYGEIF VSIHVNSAAN
TAAQGTETYY AKTPGDMYEE DIDLATFVNN QIVNNLNMKN RKVKEEKHIV SANTNIPAIL
VELGFLTNSE DRAKMTDDQY VEQFAESIYK GILQYYEKQ
//
