ID A0A1H3C166_9BURK Unreviewed; 324 AA.
AC A0A1H3C166;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN ORFNames=SAMN04515617_10439 {ECO:0000313|EMBL:SDX47239.1};
OS Collimonas sp. OK242.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1798195 {ECO:0000313|EMBL:SDX47239.1, ECO:0000313|Proteomes:UP000198586};
RN [1] {ECO:0000313|EMBL:SDX47239.1, ECO:0000313|Proteomes:UP000198586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK242 {ECO:0000313|EMBL:SDX47239.1,
RC ECO:0000313|Proteomes:UP000198586};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNOR01000004; SDX47239.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3C166; -.
DR STRING; 1798195.SAMN04515617_10439; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000198586; 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:SDX47239.1};
KW Cilium {ECO:0000313|EMBL:SDX47239.1};
KW Flagellum {ECO:0000313|EMBL:SDX47239.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764}.
FT DOMAIN 167..324
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 34803 MW; 3B700E5F4A208326 CRC64;
MSVSGPAGTI NGNSRSGDLD QRFALDVQGV DALRRTTRNS PQDGLKQVSR QFEAMFMQMV
LKSMREATPS DGMFDSQQEK LYTSMLDQQL AQNLSGRGLG LAEAMQAQLS RAVDPSQQQA
SPLSKMPAPL IDQHPAQPAA AATPNLNSSP ANLQNLSLYD AADYGYGRGA AGNSQAHVDQ
FLSRMSSSAQ VASQASGVPA QLILAQAALE SGWGKREIKG DDGSRSHNLF GIKAGKAWKG
PVVQAVTTEY VDGVPQQTRA SFRAYASYDE AFSDYARFLA GNPRYAQVLA TRDPAEAAHG
LQRAGYATDP QYGEKLVRIM KQIL
//
