ID A0A2S0P7R6_9NEIS Unreviewed; 311 AA.
AC A0A2S0P7R6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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:AVY93327.1};
GN ORFNames=DAI18_04160 {ECO:0000313|EMBL:AVY93327.1};
OS Microvirgula aerodenitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Microvirgula.
OX NCBI_TaxID=57480 {ECO:0000313|EMBL:AVY93327.1, ECO:0000313|Proteomes:UP000244173};
RN [1] {ECO:0000313|EMBL:AVY93327.1, ECO:0000313|Proteomes:UP000244173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BE2.4 {ECO:0000313|EMBL:AVY93327.1,
RC ECO:0000313|Proteomes:UP000244173};
RA Anderson E., Jang J., Ishii S.;
RT "Denitrifier Microvirgula.";
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}.
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DR EMBL; CP028519; AVY93327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0P7R6; -.
DR SMR; A0A2S0P7R6; -.
DR STRING; 1122240.GCA_000620105_00573; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000244173; 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:AVY93327.1};
KW Cilium {ECO:0000313|EMBL:AVY93327.1};
KW Flagellum {ECO:0000313|EMBL:AVY93327.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AVY93327.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000244173}.
FT DOMAIN 156..311
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 311 AA; 33355 MW; 9663E98B4A8D63C5 CRC64;
MASTPISQAD IGLAYDTQRL GNLKVLAKDD PKVAARKAAS EFEALFLQTL LKTMRETRFD
GEEDSNALDT YRGMADQQLA QTMAKGSGMG LGEALYQQIL KASGQAADAD APVTRNAEPV
KFNSVISPRL QAALSRAQGE EKRYEPMRAL DALEAPLAAP VGREDFVQQI APHARQAAAN
LGVTPNLVVA HAALESGWGK RNIRNADGSN SHNLFGIKAG GSWQGKTTDI VTTEYENGSP
KKKVERFRAY DNYGEAFADY AKLLQNNPRY AGALNTGADA VSFARGLARG GYATDPAYAE
KLARVATGTR S
//
