ID A0A3D8K0H5_9BURK Unreviewed; 347 AA.
AC A0A3D8K0H5;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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:RDU98345.1};
GN ORFNames=DWV00_13625 {ECO:0000313|EMBL:RDU98345.1};
OS Trinickia dinghuensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=2291023 {ECO:0000313|EMBL:RDU98345.1, ECO:0000313|Proteomes:UP000256838};
RN [1] {ECO:0000313|EMBL:RDU98345.1, ECO:0000313|Proteomes:UP000256838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHOM06 {ECO:0000313|EMBL:RDU98345.1,
RC ECO:0000313|Proteomes:UP000256838};
RA Gao Z.-H., Qiu L.-H.;
RT "Paraburkholderia sp. DHOM06 isolated from forest soil.";
RL Submitted (AUG-2018) 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:RDU98345.1}.
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DR EMBL; QRGA01000007; RDU98345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8K0H5; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000256838; 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 Cell projection {ECO:0000313|EMBL:RDU98345.1};
KW Cilium {ECO:0000313|EMBL:RDU98345.1};
KW Flagellum {ECO:0000313|EMBL:RDU98345.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:RDU98345.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000256838}.
FT DOMAIN 191..347
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 347 AA; 35620 MW; 1272A5786B40D285 CRC64;
MNPNTTYSGK VDSGTGTGTD ISQRFALDVQ GFDALRAQAG ADPKQALKST AHQFDAVFMQ
MMLKSMREAT PQDGILDSHE SAQYTSMLDQ QLSQQLSSKG VGLANQLITQ LSRNLGETEA
GGAGGAGGAG AAGMIAGGNG IGGMLGGGGA SDPGSAAMLS ALARAYSNAQ SNGSLADGKG
YSAQSALTPP LRGNGESAKV DAFVDKLAAP AQAASAATGI PARFIVGQAA LESGWGKGEI
KNADGSPSHN VFGIKATPDW TGKTVAAVTT EYVNGKAHRV VQKFRAYGSY ADAMTDYASM
LRDNPRYASV LSTSHDAVSF AHGMQKAGYA TDPHYAKKLI SIMKHMV
//
