ID   FLGJ_PSEAE              Reviewed;         400 AA.
AC   Q9I4P4;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Peptidoglycan hydrolase FlgJ;
DE            EC=3.2.1.-;
DE   AltName: Full=Muramidase FlgJ;
GN   Name=flgJ; OrderedLocusNames=PA1085;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Flagellum-specific muramidase which hydrolyzes the
CC       peptidoglycan layer to assemble the rod structure in the periplasmic
CC       space. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: Probably exported via the flagellum-specific export
CC       pathway.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the FlgJ family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the glycosyl
CC       hydrolase 73 family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG04474.1; -; Genomic_DNA.
DR   PIR; C83511; C83511.
DR   RefSeq; NP_249776.1; NC_002516.2.
DR   RefSeq; WP_003112508.1; NZ_QZGE01000006.1.
DR   AlphaFoldDB; Q9I4P4; -.
DR   SMR; Q9I4P4; -.
DR   STRING; 287.DR97_858; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   PaxDb; Q9I4P4; -.
DR   EnsemblBacteria; AAG04474; AAG04474; PA1085.
DR   GeneID; 878578; -.
DR   KEGG; pae:PA1085; -.
DR   PATRIC; fig|208964.12.peg.1124; -.
DR   PseudoCAP; PA1085; -.
DR   HOGENOM; CLU_013771_3_0_6; -.
DR   InParanoid; Q9I4P4; -.
DR   OMA; EGVFVQM; -.
DR   PhylomeDB; Q9I4P4; -.
DR   BioCyc; PAER208964:G1FZ6-1108-MON; -.
DR   Proteomes; UP000002438; 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:0071973; P:bacterial-type flagellum-dependent cell motility; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR019301; Flagellar_prot_FlgJ_N.
DR   InterPro; IPR013377; FlaJ.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF10135; Rod-binding; 1.
DR   SMART; SM00047; LYZ2; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   TIGRFAMs; TIGR02541; flagell_FlgJ; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum biogenesis; Cell wall biogenesis/degradation;
KW   Glycosidase; Hydrolase; Periplasm; Reference proteome.
FT   CHAIN           1..400
FT                   /note="Peptidoglycan hydrolase FlgJ"
FT                   /id="PRO_0000165707"
FT   REGION          112..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..400
FT                   /note="Catalytic"
FT   COMPBIAS        204..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        335
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   400 AA;  43156 MW;  6E96ADEC717A1F7D CRC64;
     MDSRLLSGIG AGPDSGSYTD LNRLNQLKVG KDRDGEANIR KVAQEFESLF LNEMLKSMRS
     ANEALGDGNF MNSQTTKQYQ DMYDQQLSVS LSKNAGGIGL ADVLVRQLSK MKQGSRGNGE
     NPFARVAENG AGRWPSNPSA QAGKALPMPE AGRDDSKLLN QRRLALPGKL AERMLAGIVP
     SASPAASQMQ SLGQDSYLPA QSYPAASRRG FSTDGVDSQG SRRIAQPPLA RGKSMFASAD
     EFIATMLPMA QKAAERIGVD ARYLVAQAAL ETGWGKSIIR QQDGGSSHNL FGIKTGSRWD
     GASARALTTE YEGGKAVKEI AAFRSYSSFE QSFHDYVSFL QGNDRYQNAL DSAANPERFM
     QELQRAGYAT DPQYARKVAQ IARQMQTYQA VAAAGTPPLG