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Database: UniProt
Entry: A0A1H9BS97_9LACT
LinkDB: A0A1H9BS97_9LACT
Original site: A0A1H9BS97_9LACT 
ID   A0A1H9BS97_9LACT        Unreviewed;       784 AA.
AC   A0A1H9BS97;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Flagellum-specific peptidoglycan hydrolase FlgJ {ECO:0000313|EMBL:SEP91864.1};
GN   ORFNames=SAMN04488558_10386 {ECO:0000313|EMBL:SEP91864.1};
OS   Ignavigranum ruoffiae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Ignavigranum.
OX   NCBI_TaxID=89093 {ECO:0000313|EMBL:SEP91864.1, ECO:0000313|Proteomes:UP000198833};
RN   [1] {ECO:0000313|EMBL:SEP91864.1, ECO:0000313|Proteomes:UP000198833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15695 {ECO:0000313|EMBL:SEP91864.1,
RC   ECO:0000313|Proteomes:UP000198833};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC       {ECO:0000256|ARBA:ARBA00010266}.
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DR   EMBL; FOEN01000003; SEP91864.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9BS97; -.
DR   STRING; 89093.SAMN04488558_10386; -.
DR   Proteomes; UP000198833; 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   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   PRINTS; PR01002; FLGFLGJ.
DR   SMART; SM00047; LYZ2; 1.
DR   SUPFAM; SSF52266; SGNH hydrolase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SEP91864.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198833};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          2..152
FT                   /note="Mannosyl-glycoprotein endo-beta-N-
FT                   acetylglucosamidase-like"
FT                   /evidence="ECO:0000259|SMART:SM00047"
FT   REGION          157..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..179
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  88426 MW;  28E7CA2EC97763D3 CRC64;
     MGYLEDVKPG AIAGWHNYKV LPSVTGAQAV LESGWGKSKL AQPPYNNNFG IKASSDWTGR
     VVNMQTREVI NGVSQWVYAD FRAYDSLADS IEDHAAFFTN TEWRRNHYKA VIGETDYKKA
     CWALQNAGYA TDPGYATSLI RVIEQNKLYE WDQEAFSGKS SDGSSNNTSG TTSGNLQPID
     KKVGGNLSDA ARSAVRNIGV SVIGDSLGVG TKPYLHKLLP DSNYDVYGSR QITHSDPIYS
     GMESLKKMKN AGTLKNIIVV ILGTNRGLER TEVEEFMMLA GESRKVIWVN TLSMVNHQYK
     VDEVTHWASK TFKNAFLADW LSFANAMRKT WYGSDNIHMI PEGYKKHAEF IAQAVYEAST
     ADFSTRKAEK SVTEYHTIKG FKLSEDGILK YTSYDTDGNK TENEVQTHYR GLATNGVDSC
     IYNREANNKW NIQGQTIKAK WIEQDFQADK ASLPLIYEAL EFMNKHKEPA MTYRINLYDM
     PETISIGDWG LFIDHEFNPP LYLHARVEEI VESQTNKSLN SVVISNVREL LAPEKSLVVQ
     IQEELQKERT KLLNEWRKGE PIKLELSASN GLILDDKVTE TTIAAKIYQG TKDVTEVFSD
     FRWERVSQER ELDTEFNNRL SETENTSLLK VYKQDIIGSE TTFICRVYDD SGQLVGQAGV
     SLTIPSKGRD GKNYITYIAY ANSDDGTKDF SRTETNRDYM GQYVREATKN LVLNPGPVKL
     TKPQGYVDIK PVVNLEYGKY YVLSFEPTFE SDGTTSWEIA DGNEVHTHIG EWSANPTYIF
     EGVE
//
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