ID   FLGJ_ECOLI              Reviewed;         313 AA.
AC   P75942;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   24-JAN-2024, entry version 153.
DE   RecName: Full=Peptidoglycan hydrolase FlgJ;
DE            EC=3.2.1.-;
DE   AltName: Full=Muramidase FlgJ;
GN   Name=flgJ; Synonyms=fla FX, flaZ; OrderedLocusNames=b1081, JW1068;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U00096; AAC74165.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35890.1; -; Genomic_DNA.
DR   PIR; F64851; F64851.
DR   RefSeq; NP_415599.1; NC_000913.3.
DR   RefSeq; WP_001295441.1; NZ_SSZK01000053.1.
DR   AlphaFoldDB; P75942; -.
DR   SMR; P75942; -.
DR   BioGRID; 4261020; 118.
DR   IntAct; P75942; 11.
DR   STRING; 511145.b1081; -.
DR   CAZy; GH73; Glycoside Hydrolase Family 73.
DR   PaxDb; 511145-b1081; -.
DR   EnsemblBacteria; AAC74165; AAC74165; b1081.
DR   GeneID; 75171206; -.
DR   GeneID; 947456; -.
DR   KEGG; ecj:JW1068; -.
DR   KEGG; eco:b1081; -.
DR   PATRIC; fig|1411691.4.peg.1187; -.
DR   EchoBASE; EB4020; -.
DR   eggNOG; COG1705; Bacteria.
DR   eggNOG; COG3951; Bacteria.
DR   HOGENOM; CLU_013771_3_0_6; -.
DR   InParanoid; P75942; -.
DR   OMA; EGVFVQM; -.
DR   OrthoDB; 289937at2; -.
DR   PhylomeDB; P75942; -.
DR   BioCyc; EcoCyc:G366-MONOMER; -.
DR   PRO; PR:P75942; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; 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; IMP:EcoCyc.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; Cell wall biogenesis/degradation;
KW   Glycosidase; Hydrolase; Periplasm; Reference proteome.
FT   CHAIN           1..313
FT                   /note="Peptidoglycan hydrolase FlgJ"
FT                   /id="PRO_0000165705"
FT   REGION          148..313
FT                   /note="Catalytic"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        245
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   313 AA;  34475 MW;  C4B3CB8F36751CDF CRC64;
     MISDSKLLAS AAWDAQSLNE LKAKAGEDPA ANIRPVARQV EGMFVQMMLK SMRDALPKDG
     LFSSEHTRLY TSMYDQQIAQ QMTAGKGLGL AEMMVKQMTP EQPLPEESTP AAPMKFPLET
     VVRYQNQALS QLVQKAVPRN YDDSLPGDSK AFLAQLSLPA QLASQQSGVP HHLILAQAAL
     ESGWGQRQIR RENGEPSYNL FGVKASGNWK GPVTEITTTE YENGEAKKVK AKFRVYSSYL
     EALSDYVGLL TRNPRYAAVT TAASAEQGAQ ALQDAGYATD PHYARKLTNM IQQMKSISDK
     VSKTYSMNID NLF
//