ID D3V2X1_XENBS Unreviewed; 321 AA.
AC D3V2X1;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN Name=flgJ {ECO:0000313|EMBL:CBJ81086.1};
GN OrderedLocusNames=XBJ1_1960 {ECO:0000313|EMBL:CBJ81086.1};
OS Xenorhabdus bovienii (strain SS-2004).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ81086.1, ECO:0000313|Proteomes:UP000002045};
RN [1] {ECO:0000313|EMBL:CBJ81086.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ81086.1};
RX PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA Goodrich-Blair H.;
RT "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT convergent lifestyles from divergent genomes.";
RL PLoS ONE 6:E27909-E27909(2011).
CC -!- FUNCTION: Flagellum-specific muramidase which hydrolyzes the
CC peptidoglycan layer to assemble the rod structure in the periplasmic
CC space. {ECO:0000256|ARBA:ARBA00002954}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC hydrolase 73 family. {ECO:0000256|ARBA:ARBA00007974}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the FlgJ family.
CC {ECO:0000256|ARBA:ARBA00006880}.
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DR EMBL; FN667741; CBJ81086.1; -; Genomic_DNA.
DR RefSeq; WP_012988439.1; NC_013892.1.
DR AlphaFoldDB; D3V2X1; -.
DR STRING; 406818.XBJ1_1960; -.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR KEGG; xbo:XBJ1_1960; -.
DR PATRIC; fig|406818.4.peg.1771; -.
DR eggNOG; COG1705; Bacteria.
DR eggNOG; COG3951; Bacteria.
DR HOGENOM; CLU_013771_3_0_6; -.
DR Proteomes; UP000002045; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.10.70.40; peptidoglycan hydrolase; 1.
DR InterPro; IPR019301; Flagellar_prot_FlgJ_N.
DR InterPro; IPR013377; FlaJ.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR NCBIfam; TIGR02541; flagell_FlgJ; 1.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF10135; Rod-binding; 1.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00047; LYZ2; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Cell projection {ECO:0000313|EMBL:CBJ81086.1};
KW Cilium {ECO:0000313|EMBL:CBJ81086.1};
KW Flagellum {ECO:0000313|EMBL:CBJ81086.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764}.
FT DOMAIN 150..314
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 321 AA; 35383 MW; 2974D70EC4B739DB CRC64;
MSDFLTTPTA AYDVNSLHSL KAKLSQEPQQ GLRQVAQELE GVFVQMMLKS MRSSLPQDGI
LSSDQTRFYT SMYDQQIAQD LSQKGLGFAD MIVKQFSNAN NVASEQAGTV PMPLDKEFLQ
TLPKQALEQF MRRTMTAPFS SAASKGSVQS KSLPVSSTDF VSMLSLPAQI ASQQSGIPHL
LIIAQAALES GWGQREILTE EGKPSHNLFG IKAGKHWKGA VTNIMTTEYI EGEPKKMHDS
FRVYGSYREA ITDYVKLLTE NPRYAKVAQS TTAEQGAYSL QSAGYATDPG YAKKLVSLIQ
QLKSTGNQMV KAYTDDFDNL F
//
