ID   FLGJ_VIBPA              Reviewed;         308 AA.
AC   Q9X9J3;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Peptidoglycan hydrolase FlgJ;
DE            EC=3.2.1.-;
DE   AltName: Full=Muramidase FlgJ;
GN   Name=flgJ; OrderedLocusNames=VP0784;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB22;
RA   McCarter L.L.;
RT   "Polar flagellar region I.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; U12817; AAD42920.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC59047.1; -; Genomic_DNA.
DR   RefSeq; NP_797163.1; NC_004603.1.
DR   RefSeq; WP_005454015.1; NC_004603.1.
DR   AlphaFoldDB; Q9X9J3; -.
DR   SMR; Q9X9J3; -.
DR   STRING; 223926.28805770; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   EnsemblBacteria; BAC59047; BAC59047; BAC59047.
DR   GeneID; 1188281; -.
DR   KEGG; vpa:VP0784; -.
DR   PATRIC; fig|223926.6.peg.749; -.
DR   eggNOG; COG1705; Bacteria.
DR   eggNOG; COG3951; Bacteria.
DR   HOGENOM; CLU_013771_3_0_6; -.
DR   OMA; EGVFVQM; -.
DR   Proteomes; UP000002493; Chromosome 1.
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: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; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   Pfam; PF10135; Rod-binding; 1.
DR   SMART; SM00047; LYZ2; 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..308
FT                   /note="Peptidoglycan hydrolase FlgJ"
FT                   /id="PRO_0000165710"
FT   REGION          159..308
FT                   /note="Catalytic"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        255
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   308 AA;  34524 MW;  8DD0652D84AE88E1 CRC64;
     MMKNPNDIGF IHDISSLDSL RQKAVKEGKD GEQEALHAAA RQFESIFTSM MLKSMREANE
     GFESNIMNSQ NEKFYRQMLD EQMASELSAN GSMGLADMIV AQLTAGQGND KSETAMRDAA
     NSAVEYRRVD PKKAREIEKR LIESGELSRT SHTPAKFDSP ESFVNSMKPY AEKAAKALGV
     EPSLLLAQAA LETGWGQKVV QNARGSSNNL FNIKADRSWQ GDKVTTQTLE FHDNTPVKET
     AAFRSYSNYQ DSFNDYVRFL NDNPRYETAL QQRGDSESFI RGIHRAGYAT DPTYADKVLQ
     VKQKIESM