ID Q1GBZ0_LACDA Unreviewed; 401 AA.
AC Q1GBZ0;
DT 27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 27-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Putative amidase {ECO:0000313|EMBL:CAI97064.1};
GN OrderedLocusNames=Ldb0224 {ECO:0000313|EMBL:CAI97064.1};
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333 {ECO:0000313|EMBL:CAI97064.1, ECO:0000313|Proteomes:UP000001259};
RN [1] {ECO:0000313|EMBL:CAI97064.1, ECO:0000313|Proteomes:UP000001259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 /
RC NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14
RC {ECO:0000313|Proteomes:UP000001259};
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC {ECO:0000256|ARBA:ARBA00010266}.
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DR EMBL; CR954253; CAI97064.1; -; Genomic_DNA.
DR RefSeq; WP_011543567.1; NZ_JQAV01000003.1.
DR AlphaFoldDB; Q1GBZ0; -.
DR STRING; 390333.Ldb0224; -.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR KEGG; ldb:Ldb0224; -.
DR PATRIC; fig|390333.13.peg.1253; -.
DR eggNOG; COG1705; Bacteria.
DR HOGENOM; CLU_056346_0_0_9; -.
DR BioCyc; LDEL390333:LDB_RS00950-MONOMER; -.
DR Proteomes; UP000001259; Chromosome.
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 InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR InterPro; IPR024968; SlpA_dom.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF03217; SlpA; 2.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00047; LYZ2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001259};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..401
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039572244"
FT DOMAIN 26..194
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 401 AA; 43042 MW; 984C66111F577A6B CRC64;
MKRRFLTGLA TAAMLTSVAV PVTNNMFLSN QAVEASATSD AFLSKVSLQA QKTSKKYGVY
ASLMLAQAAL ESGWGTSTLS TQANNFFGMK ATGWTGATYS VKTAEQTSSG KTYYITAAFR
KYSSYQASFD DYGLKMRTTL GNYGSLCYSK TWLENASSAS AAAKAIKAAG YATDTNYATK
LISHIGTYNL TKYDPVYSGT NYTAKVAKSG ATYLYPTDHS VSPKKSYVTA GQTVTVTKTY
TYYNGKKRMY LKGLGWINGE SLNTGSSQAP SAADNAASVS GQMKVLMHSA AIYTSTGAKS
TAKSVKAGKS VTTYGSVTIN GAKYYRVNSA SADQFIKASN FDGTSRKLKR NAYIYNNAGK
RVGKTKWLKG STHTVYGGSV KIKGKQYCIV GLNQYVKKAN F
//
