FLGJ_ECO57
ID FLGJ_ECO57 Reviewed; 313 AA.
AC P58231;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Peptidoglycan hydrolase FlgJ;
DE EC=3.2.1.-;
DE AltName: Full=Muramidase FlgJ;
GN Name=flgJ; Synonyms=fla FX, flaZ; OrderedLocusNames=Z1719, ECs1459;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG55827.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34882.1; -; Genomic_DNA.
DR PIR; C90811; C90811.
DR PIR; G85670; G85670.
DR RefSeq; NP_309486.1; NC_002695.1.
DR RefSeq; WP_001301817.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P58231; -.
DR SMR; P58231; -.
DR STRING; 155864.EDL933_1658; -.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR EnsemblBacteria; AAG55827; AAG55827; Z1719.
DR EnsemblBacteria; BAB34882; BAB34882; ECs_1459.
DR GeneID; 912388; -.
DR KEGG; ece:Z1719; -.
DR KEGG; ecs:ECs_1459; -.
DR PATRIC; fig|386585.9.peg.1560; -.
DR eggNOG; COG1705; Bacteria.
DR eggNOG; COG3951; Bacteria.
DR HOGENOM; CLU_013771_3_0_6; -.
DR OMA; EGVFVQM; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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: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..313
FT /note="Peptidoglycan hydrolase FlgJ"
FT /id="PRO_0000165706"
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; 34535 MW; CEB3D7E9D05C73AA CRC64;
MISDSKLLAS AAWDAQSLNE LKAKASEDPA ANIRPVARQV EGMFVQMMLK SMRDALPKDG
LFSSEHTRLY TSMYDQQIAQ QMTTGKGLGL AEMMVKQMTP EQPLPEESTP AAPMKFPLET
VVRYQNQALS QLVQKAVPRN YDDSLPGDSK AFLAQLSLPA QLASQQSGVP HHLILAQAAL
ESGWGQRQIR RENGEPSYNL FGVKASGNWK GPVTEITTTE YENGEAKKVK AKFRVYSSYL
EALSDYVGLL TRNPRYAAVT TAASAEQGAQ ALQDAGYATD PHYARKLTNM IQQMKSISDK
VSKTYSMNID NLF