ID W1IM48_9GAMM Unreviewed; 331 AA.
AC W1IM48;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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:CDL79504.1};
GN ORFNames=XCR1_1160017 {ECO:0000313|EMBL:CDL79504.1};
OS Xenorhabdus cabanillasii JM26.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427517 {ECO:0000313|EMBL:CDL79504.1, ECO:0000313|Proteomes:UP000019197};
RN [1] {ECO:0000313|EMBL:CDL79504.1, ECO:0000313|Proteomes:UP000019197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM26 {ECO:0000313|EMBL:CDL79504.1,
RC ECO:0000313|Proteomes:UP000019197};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacterium,
RT Xenorhabdus cabanillasi strain JM26.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:CDL79504.1}.
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DR EMBL; CBXE010000020; CDL79504.1; -; Genomic_DNA.
DR RefSeq; WP_038259971.1; NZ_NJGH01000053.1.
DR AlphaFoldDB; W1IM48; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000019197; Unassembled WGS sequence.
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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CDL79504.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CDL79504.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764}.
FT DOMAIN 160..324
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 331 AA; 36610 MW; 7B77FF8969A3858A CRC64;
MNDFLTMPNV AYDVNSLHSL KAKLSQEPQQ GLRQVAQQLE GVFVQIMLKS MRSSLPQDGI
LSSDQTRFYT SMYDQQIAQD LSQKGLGFAD MIVKQFSNAI PNTVPNISSV PSELAGTVPM
PLDNEILHTL PKQALEQFLR RTMPDKSPNR AAQSKTLPMT RSLPINSASF VSMLSVPAQI
ASQQSGIPHL LIIAQAALES GWGQREILTE EGKPSHNLFG IKAGKSWQGP VTQITTTEYI
DGEPKTIRDS FRVYDSYLDA VTDYVKLLAE NPRYAKVARS TTAEQGAYSL QDAGYATDPG
YAEKLVSLIR QLKSSGNQMV KAYHDDFDNL F
//
