ID A0A410USM3_9BURK Unreviewed; 339 AA.
AC A0A410USM3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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:QAU34350.1};
GN ORFNames=EKL02_09250 {ECO:0000313|EMBL:QAU34350.1};
OS Janthinobacterium sp. 17J80-10.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=2497863 {ECO:0000313|EMBL:QAU34350.1, ECO:0000313|Proteomes:UP000288813};
RN [1] {ECO:0000313|EMBL:QAU34350.1, ECO:0000313|Proteomes:UP000288813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17J80-10 {ECO:0000313|EMBL:QAU34350.1,
RC ECO:0000313|Proteomes:UP000288813};
RA Kim M., Maeng S., Sathiyaraj S.;
RT "genome sequence of Janthinobacteria sp. 17J80-10.";
RL Submitted (JAN-2019) 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}.
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DR EMBL; CP035311; QAU34350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410USM3; -.
DR KEGG; jaj:EKL02_09250; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000288813; 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:QAU34350.1};
KW Cilium {ECO:0000313|EMBL:QAU34350.1};
KW Flagellum {ECO:0000313|EMBL:QAU34350.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:QAU34350.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000288813}.
FT DOMAIN 182..338
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT REGION 100..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 36067 MW; C4EBD4230DC5B6A2 CRC64;
MSNSVDFSGK LALDSRGLGA LRESARQQSP ESIKAAAKQF EALFMNMVMK SMREATPQDG
MFDNQQTKMY TSMLDQQLSQ TLANRGVGLA DVLARQLSAN RGLPPPAPGE AGDAGNAATG
GAAADGISGM APVRQLNPQR QAQIAAFQEQ LRLQNEEGGS GMTPGGMPGQ AGSASGVAEA
GKSRSRHAHV RAFEDRLAHH ADEASRATGI PAKFMLGQAA LETGWGKREI RGADGSNSFN
LFGIKATGGW KGKVVEVATT EYVNGAPQIK REKFRAYDSY ADSFRDYARL LGQNPRYENV
IANAQDASGF AHGLQRAGYA TDPQYAAKLT RIIQQTLSA
//
