ID A0A1U9N7G6_9GAMM Unreviewed; 397 AA.
AC A0A1U9N7G6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptidoglycan hydrolase FlgJ {ECO:0000256|ARBA:ARBA00013433};
DE AltName: Full=Muramidase FlgJ {ECO:0000256|ARBA:ARBA00030835};
GN ORFNames=B0D95_04590 {ECO:0000313|EMBL:AQT59445.1};
OS Cellvibrio sp. PSBB023.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=1945512 {ECO:0000313|EMBL:AQT59445.1, ECO:0000313|Proteomes:UP000189646};
RN [1] {ECO:0000313|EMBL:AQT59445.1, ECO:0000313|Proteomes:UP000189646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PSBB023 {ECO:0000313|EMBL:AQT59445.1,
RC ECO:0000313|Proteomes:UP000189646};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; CP019799; AQT59445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U9N7G6; -.
DR STRING; 1945512.B0D95_04590; -.
DR KEGG; ceb:B0D95_04590; -.
DR OrthoDB; 289937at2; -.
DR Proteomes; UP000189646; 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 SMART; SM00047; LYZ2; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795};
KW Cell projection {ECO:0000313|EMBL:AQT59445.1};
KW Cilium {ECO:0000313|EMBL:AQT59445.1};
KW Flagellum {ECO:0000313|EMBL:AQT59445.1};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000189646}.
FT DOMAIN 205..369
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
SQ SEQUENCE 397 AA; 43739 MW; 9E539998E94517D2 CRC64;
MQSIDTGIKV PQVQDNYFDP NSLNSIKAMG RDRDPQAIKE VAKKFEGLLV QQMLKSMREA
NDVFGEGSFL DSQTTRFHRD MLDQQMVLDL TSGPGIGLAD HFYRQMMQNY GSTMRPEGGV
KNTDSSALGE ITPRTANKTS VAEQASVDAL DDWIQDFMRM SDNVQMQALG DGDEQQVPAV
PAINYALIPQ LLSKQAIGTV RGGQKSSISP TQENFVMMLK PHAERAAAEL QISPDVLIAQ
VALETGWGKH VIHDRSGNNS FNLFNIKAGG QWQGEKVNVN TLEYRNGIAA QEKSDFRKYN
DYSESFSDYV RLMKNNPRYE KVLATGTNSS AYADALQSAG YATDPHYAKK IKSLLNSDVI
KSLDLASVTE NMQADLLQTG AQAILSLAAS ASRHIVE
//
