ID A0A2U2HGN9_9BURK Unreviewed; 345 AA.
AC A0A2U2HGN9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
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:PWF44350.1};
GN ORFNames=C7C56_019530 {ECO:0000313|EMBL:PWF44350.1};
OS Massilia glaciei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1524097 {ECO:0000313|EMBL:PWF44350.1, ECO:0000313|Proteomes:UP000241421};
RN [1] {ECO:0000313|EMBL:PWF44350.1, ECO:0000313|Proteomes:UP000241421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B448-2 {ECO:0000313|EMBL:PWF44350.1,
RC ECO:0000313|Proteomes:UP000241421};
RA Wang H.;
RT "Massilia violaceinigra sp. nov., a novel purple-pigmented bacterium
RT isolated from Tianshan glacier, Xinjiang, China.";
RL Submitted (APR-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:PWF44350.1}.
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DR EMBL; PXWF02000269; PWF44350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2HGN9; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000241421; 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:PWF44350.1};
KW Cilium {ECO:0000313|EMBL:PWF44350.1};
KW Flagellum {ECO:0000313|EMBL:PWF44350.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:PWF44350.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000241421}.
FT DOMAIN 190..344
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 345 AA; 36522 MW; DF97518CE03AEA20 CRC64;
MDSLKHDLSS RLAFDSQGLG ALKASAKAGS PDALKAASTQ FEAMFINMMM KSMRAATPQD
GMFDSEQSKM FTSMLDQQTS ENLAKRGVGL ADVLIRQLSS QALGGRDVGP GEGGSVAQGR
GMPQQFLAEP VNAQALAIGG DSVKQPGAGV PYTDVFKMHP IIKDALAGVL PAAPAGPAWS
AAQLQDGPRL ASQQEHVRAF QNKLGGHAEE ASRVSGIPAK FMLGQAALES GWGKREIQNA
DGSASHNLFG IKAGPGWKGR VATATTTEYV NGVPQTRVER FRAYDSYADS FNDFARMIST
NPRYEKVLAA AGDASSFAHG LQKAGYATDP RYGEKLSRII RQSLG
//
