ID   FLGJ_VIBCH              Reviewed;         334 AA.
AC   Q9KQ15; O30855;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Peptidoglycan hydrolase FlgJ;
DE            EC=3.2.1.-;
DE   AltName: Full=Muramidase FlgJ;
GN   Name=flgJ; OrderedLocusNames=VC_2192;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=El Tor Inaba V86;
RX   PubMed=9742694; DOI=10.1111/j.1574-6968.1998.tb13152.x;
RA   Das M., Chopra A.K., Wood T., Peterson J.W.;
RT   "Cloning, sequencing and expression of the flagellin core protein and other
RT   genes encoding structural proteins of the Vibrio cholerae flagellum.";
RL   FEMS Microbiol. Lett. 165:239-246(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(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; AF019213; AAC33157.1; -; Genomic_DNA.
DR   EMBL; AE003852; AAF95337.1; -; Genomic_DNA.
DR   PIR; G82105; G82105.
DR   RefSeq; NP_231823.1; NC_002505.1.
DR   AlphaFoldDB; Q9KQ15; -.
DR   SMR; Q9KQ15; -.
DR   STRING; 243277.VC_2192; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   DNASU; 2613232; -.
DR   EnsemblBacteria; AAF95337; AAF95337; VC_2192.
DR   KEGG; vch:VC_2192; -.
DR   PATRIC; fig|243277.26.peg.2089; -.
DR   eggNOG; COG1705; Bacteria.
DR   eggNOG; COG3951; Bacteria.
DR   HOGENOM; CLU_013771_3_0_6; -.
DR   OMA; EGVFVQM; -.
DR   Proteomes; UP000000584; 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: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; 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..334
FT                   /note="Peptidoglycan hydrolase FlgJ"
FT                   /id="PRO_0000165709"
FT   REGION          160..334
FT                   /note="Catalytic"
FT   ACT_SITE        231
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000255"
FT   CONFLICT        90
FT                   /note="S -> C (in Ref. 1; AAC33157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312..334
FT                   /note="YKSPAGIFRRHSFSSSIFSAYQS -> L (in Ref. 2; AAF95337)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  37271 MW;  DEA90D8B0745450A CRC64;
     MINNSNDIGF IQDIAGLDKL RQKAVNGDEN AGQSALTAAA RQFESIFTSM MLKSMRDANS
     DFKSDLMSSQ NEDLYRQMLD EQMASEFSSS GSLGLADMIV AQLSTGQTAS EQKGEDGFQE
     AMRRVEHARK TASERSNEDL VAAVYPLRKT QAVQSTQFDS RHSFVTKLKP YADKAARMLG
     VDSSLLIAQA ALETGWGQKM VKNARGNSNN LFNIKADRSW QGDKVATQTL EYHNNVPVVE
     KAAFRSYASF DESFNDYVRF LENNPRYTNA LDHGGNSERF IHGIHRAGYA TDPQYADKVL
     RVKAQIDQMN LYKSPAGIFR RHSFSSSIFS AYQS