ID A0A0F4KWY1_9LACO Unreviewed; 603 AA.
AC A0A0F4KWY1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cell wall hydrolase/muramidase {ECO:0000313|EMBL:KJY51102.1};
GN Name=acm2 {ECO:0000313|EMBL:KJY51102.1};
GN ORFNames=JG29_01450 {ECO:0000313|EMBL:KJY51102.1};
OS Bombilactobacillus mellis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1218508 {ECO:0000313|EMBL:KJY51102.1, ECO:0000313|Proteomes:UP000033695};
RN [1] {ECO:0000313|EMBL:KJY51102.1, ECO:0000313|Proteomes:UP000033695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hon2 {ECO:0000313|EMBL:KJY51102.1,
RC ECO:0000313|Proteomes:UP000033695};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC {ECO:0000256|ARBA:ARBA00010266}.
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:KJY51102.1}.
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DR EMBL; JXBZ01000002; KJY51102.1; -; Genomic_DNA.
DR RefSeq; WP_052696260.1; NZ_KQ033877.1.
DR AlphaFoldDB; A0A0F4KWY1; -.
DR STRING; 1218508.JG29_01450; -.
DR PATRIC; fig|1218508.4.peg.150; -.
DR HOGENOM; CLU_021790_0_0_9; -.
DR OrthoDB; 37530at2; -.
DR Proteomes; UP000033695; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 4.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR InterPro; IPR003646; SH3-like_bac-type.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF08460; SH3_5; 4.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00047; LYZ2; 1.
DR SMART; SM00287; SH3b; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KJY51102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033695};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..603
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002471835"
FT DOMAIN 118..270
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT DOMAIN 294..359
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
FT DOMAIN 372..437
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
FT DOMAIN 461..529
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
FT DOMAIN 542..601
FT /note="SH3b"
FT /evidence="ECO:0000259|SMART:SM00287"
FT REGION 29..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 65206 MW; 2FDCECBE5A8D42F2 CRC64;
MKKNNLFWSA VLVSATILTT LPAQNAKADN NNLAPQLNNN QSVEPATTNN SNDSAANINS
SSANQADSQT NTTSSNNSIS APASSATTDN SNNNFATRAA VASANTANTD NSINTFSTIS
NYLSPASFLS QIKPGSISGW QQYHILPSIT AAQAILESGW GNSQLAQQYH NLFGIKGSNN
GQSVTLPTNE EVSGNTININ AQFRAYSSWA ESITDHGVFL NSNSRYHNIL GVTNYRQVAQ
LLQQDGYATS SSYAQYLINI IESNNLQAWD QEALGQGSNN SNSQPVVPNN NQNNGTYTFT
QATNIYTSTS THGQVVGQYQ KGQTVIYNDK IQAEGLTWLR YTSYSGKTCY VPINSNNGNQ
STTPNTPAVN DSNGVYTFQV DTNIRTSPSL QGTIIGRYAT GQHVYYNGKV NADGYIWLKY
LSSSGKTCYV AMVAADYSPL LDNSSNNSNK TPHDNQSTVQ NESGVYTFPK TTNIYTETNL
NSKVVGHYAA GQRVFYNGKV NANGTSWLRY LSYSGTTCYV PLNNEQKPAA TSTPGTSPIA
NYGTYTFKVA TNIRLKPSLQ GKIVGSYNAG QKVFYNGKVV GDGYTWLYYL SYSGTTCYVA
VIG
//
