ID A0A368L3Q8_9BURK Unreviewed; 335 AA.
AC A0A368L3Q8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:RCS58194.1};
GN ORFNames=DU000_05045 {ECO:0000313|EMBL:RCS58194.1};
OS Parvibium lacunae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Parvibium.
OX NCBI_TaxID=1888893 {ECO:0000313|EMBL:RCS58194.1, ECO:0000313|Proteomes:UP000252357};
RN [1] {ECO:0000313|EMBL:RCS58194.1, ECO:0000313|Proteomes:UP000252357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMB9 {ECO:0000313|EMBL:RCS58194.1,
RC ECO:0000313|Proteomes:UP000252357};
RX PubMed=29498621; DOI=10.1099/ijsem.0.002667;
RA Chen W.M., Xie P.B., Hsu M.Y., Sheu S.Y.;
RT "Parvibium lacunae gen. nov., sp. nov., a new member of the family
RT Alcaligenaceae isolated from a freshwater pond.";
RL Int. J. Syst. Evol. Microbiol. 68:1291-1299(2018).
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:RCS58194.1}.
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DR EMBL; QPGB01000002; RCS58194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A368L3Q8; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000252357; 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; IPR023346; Lysozyme-like_dom_sf.
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.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Cell projection {ECO:0000313|EMBL:RCS58194.1};
KW Cilium {ECO:0000313|EMBL:RCS58194.1};
KW Flagellum {ECO:0000313|EMBL:RCS58194.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RCS58194.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000252357}.
FT DOMAIN 177..331
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT REGION 150..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 335 AA; 36806 MW; 5769BC0B7E2ED695 CRC64;
MTQSSSLYPT AVTLSASDFR GSAKPLSATD GNNLEDLKRI ARDNPEAAVR AAAKQFEAVF
LQMVLKSMRA TEMKSGLLES SSGDMFQGMY DEQLTKTLSQ RGVGLADMLE KQLMRQIKPE
QANPTLPIKP LLRPDQSTWN PVSTLEKLNR ATQEAQQATQ GISRPELTSP KNGVSNTNST
TAAPREFVQR LWQEAKQAEQ QVGIPAQFML GQAALESGWG KREIKFANGD PSHNLFGIKA
GPGWRGKVVE TVTTEYINGV PKQVTEKFRA YDSYAAAFND YARLISQNPR YKQALQEVDS
AAGYAAQLQK AGYATDPYYA TKLTKTIATT LRVIA
//
